Gene_locus Report for: yarli-q6cep3 Yarrowia lipolytica (Candida lipolytica) lipolytica
Relationship
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Fungi: N E > Dikarya: N E > Ascomycota: N E > saccharomyceta: N E > Saccharomycotina: N E > Saccharomycetes: N E > Saccharomycetales: N E > Dipodascaceae: N E > Yarrowia: N E > Yarrowia lipolytica: N E
6_AlphaBeta_hydrolase :
yarli-q6ceg0 Yarrowia lipolytica (Candida lipolytica) similar to ca2278|ipf10806 candida albicans unknown function .
A85-EsteraseD-FGH :
yarli-q6cbb1 Yarrowia lipolytica (Candida lipolytica) similar to sp|p10768 homo sapiens esterase d .
ABHD11-Acetyl_transferase :
yarli-q6c9u0 Yarrowia lipolytica (Candida lipolytica) b11c21.140 .
ABHD13-BEM46 :
yarli-q6c7y6 Yarrowia lipolytica (Candida lipolytica) lipolytica .
abh_upf0017 :
yarli-q6ce37 Yarrowia lipolytica (Candida lipolytica) lipolytica .
Acidic_Lipase :
yarli-q6c3u6 Yarrowia lipolytica (Candida lipolytica) similar to wi|ncu02148.1 neurospora crassa ncu02148. 1 ,
yarli-q6c7i7 Yarrowia lipolytica (Candida lipolytica) similarities with tr|q07950 saccharomyces cerevisiae ylr020c .
Arb2_domain :
yarli-q6c4p0 Yarrowia lipolytica (Yeast) (Candida lipolytica). YALI0E24893p .
BD-FAE :
yarli-q6cbe6 Yarrowia lipolytica (Candida lipolytica) similarities with tr|q8nks0 pyrobaculum calidifontis esterase .
Carboxypeptidase_S10 :
yarli-q6c9r1 Yarrowia lipolytica (Candida lipolytica) carboxypeptidase y ,
yarli-q6c9v4 Yarrowia lipolytica (Candida lipolytica) carboxypeptidase y ,
yarli-q6c209 Yarrowia lipolytica (Candida lipolytica) lipolytica ,
yarli-q6cax2 Yarrowia lipolytica (Candida lipolytica) carboxypeptidase y ,
yarli-q6cb63 Yarrowia lipolytica (Candida lipolytica) carboxypeptidase y ,
yarli-q6cdg1 Yarrowia lipolytica (Candida lipolytica) similar to sp|p30574 candida albicans carboxypeptidase y ,
yarli-q6cdv9 Yarrowia lipolytica (Candida lipolytica) carboxypeptidase y ,
yarli-q6cfp3 Yarrowia lipolytica (Candida lipolytica) similar to tr|q871g2 neurospora crassa b7h23.190 ,
yarli-q6cg27 Yarrowia lipolytica (Candida lipolytica) similar to sp|p30574 candida albicans carboxypeptidase y ,
yarli-q6cgj3 Yarrowia lipolytica (Candida lipolytica) similar to sp|p30574 candida albicans carboxypeptidase y .
CGI-58_ABHD5_ABHD4 :
yarli-q6c3h1 Yarrowia lipolytica (Candida lipolytica) similar to deha0f24211g debaryomyces hansenii ipf 6233.1 ,
yarli-q6c8q4 Yarrowia lipolytica (Candida lipolytica) similar to sp|p53264 saccharomyces cerevisiae ygr110w ,
yarli-q6ccr0 Yarrowia lipolytica (Candida lipolytica) lipolytica .
Dienelactone_hydrolase :
yarli-q6bzv7 Yarrowia lipolytica (Candida lipolytica) function ,
yarli-q6cba7 Yarrowia lipolytica (Candida lipolytica) carboxymethylenebutenolidase .
DPP4N_Peptidase_S9 :
yarli-q6cfx2 Yarrowia lipolytica (Candida lipolytica) Dipeptidyl aminopeptidase type IV .
Duf_676 :
yarli-q6c3l1 Yarrowia lipolytica (Candida lipolytica) similar to klla0f16709g kluyveromyces lactis .
Duf_726 :
yarli-q6c4h8 Yarrowia lipolytica (Candida lipolytica) YALI0E26653p .
Epoxide_hydrolase :
yarli-q6c598 Yarrowia lipolytica (Candida lipolytica) epoxide hydrolase with promiscuous haloalkane dehalogenase activity. similar to wi|ncu00350.1 neurospora crassa ncu00350.1 ,
yarli-q6caz1 Yarrowia lipolytica (Candida lipolytica) (fragment) ,
yarli-q6ci59 Yarrowia lipolytica (Candida lipolytica) similar to tr|q16764 homo sapiens epoxide hydrolase .
FSH1 :
yarli-q6c8u4 Yarrowia lipolytica (Candida lipolytica) lipolytica .
Fungal_carboxylesterase_lipase :
yarli-LIP3 Yarrowia lipolytica (Candida lipolytica) carboxylesterase/lipase type b lipase 3 (EC 3.1.1.3) ,
yarli-lipa1 Yarrowia lipolytica DNA for LIP1 gene encoding lipase I protein ,
yarli-q6c6v2 Yarrowia lipolytica (Candida lipolytica) similar to sp|q99156 yarrowia lipolytica lip1 lipase 1 ,
yarli-q6cdi6 Yarrowia lipolytica (Candida lipolytica) similar to sp|q99156 yarrowia lipolytica lipase 1 .
Fusarinine_C_esterase_sidJ :
yarli-q6c6p7 Yarrowia lipolytica (Candida lipolytica). similar to deha0d18975g debaryomyces hansenii .
Homoserine_transacetylase :
yarli-q6c7h3 Yarrowia lipolytica (Candida lipolytica) acetyltransferase ,
yarli-q6cau6 Yarrowia lipolytica (Candida lipolytica) acetyltransferase .
Hormone-sensitive_lipase_like :
yarli-q6c5j1 Yarrowia lipolytica (Candida lipolytica) sensitive lipase .
Kynurenine-formamidase :
yarli-q6c748 Yarrowia lipolytica (Yeast) (Candida lipolytica). N-formylkynurenine formamidase .
LIDHydrolase :
yarli-q6c1f5 Yarrowia lipolytica (Candida lipolytica) YALI0F16731p ,
yarli-q6c1f7 Yarrowia lipolytica (Candida lipolytica) YALI0F16687p .
Lipase_3 :
yarli-atg15 Yarrowia lipolytica (Candida lipolytica) putative lipase atg15 (EC 3.1.1.3) (autophagy-related protein 15) ,
yarli-lip2 Yarrowia lipolytica lip2 gene YLLIP2,
yarli-LIP4 Yarrowia lipolytica (Candida lipolytica) lipase (EC 3.1.1.3) yllip4 protein ,
yarli-LIP5 Yarrowia lipolytica (Candida lipolytica) lipase (EC 3.1.1.3) (yllip5 protein) ,
yarli-LIP7 Yarrowia lipolytica (Candida lipolytica) lipase (EC 3.1.1.3) ,
yarli-LIP8 Yarrowia lipolytica (Candida lipolytica) lipase (EC 3.1.1.3) (yllip8 protein) lipy8p ,
yarli-q6bzp1 Yarrowia lipolytica (Candida lipolytica) similar to tr|cad70715 yarrowia lipolytica lipase (fragment) ,
yarli-q6c3i6 Yarrowia lipolytica (Candida lipolytica) similar to tr|q9p8f7 yarrowia lipolytica triacylglycerol lipase ,
yarli-q6c7j5 Yarrowia lipolytica (Candida lipolytica) lipolytica ,
yarli-q6c8m4 Yarrowia lipolytica (Candida lipolytica) similar to tr|q872l4 yarrowia lipolytica lipase ,
yarli-q6c8y2 Yarrowia lipolytica (Candida lipolytica) similar to tr|q9p8f7 yarrowia lipolytica triacylglycerol lipase ,
yarli-q6c9r0 Yarrowia lipolytica (Candida lipolytica) similar to tr|q9p8f7 yarrowia lipolytica triacylglycerol lipase Lip11 ,
yarli-q6c225 Yarrowia lipolytica (Candida lipolytica) similar to tr|q9p8f7 yarrowia lipolytica triacylglycerol lipase ,
yarli-q6c687 Yarrowia lipolytica (Candida lipolytica) similar to sp|cad70713 yarrowia lipolytica lipase lip4 ,
yarli-q6c822 Yarrowia lipolytica (Candida lipolytica) similarity ,
yarli-q6cey5 Yarrowia lipolytica (Candida lipolytica) similar to tr|q872l4 yarrowia lipolytica lip7 lipase ,
yarli-q6chb8 Yarrowia lipolytica (Candida lipolytica) similarity (fragment) .
LYsophospholipase_carboxylesterase :
yarli-apth1 Yarrowia lipolytica (Candida lipolytica) lysophospholipase acyl-protein thioesterase 1 (EC 3.1.2.-) .
Monoglyceridelipase_lysophospholip :
yarli-q6cby1 Yarrowia lipolytica (Candida lipolytica) similar to sp|p28321 saccharomyces cerevisiae ykl094w .
Palmitoyl-protein_thioesterase :
yarli-q6c1r3 Yarrowia lipolytica (Candida lipolytica) function .
PC-sterol_acyltransferase :
yarli-q6c5m4 Yarrowia lipolytica (Candida lipolytica) lipolytica. ,
yarli-q6c6m4 Yarrowia lipolytica (Candida lipolytica) lipolytica. Similar to deha0e15411g debaryomyces hansenii (fragment) .
PGAP1 :
yarli-BST1B Yarrowia lipolytica (Yeast) (Candida lipolytica) GPI inositol-deacylase B ,
yarli-q6c2z2 Yarrowia lipolytica (Candida lipolytica) lipolytica ,
yarli-q6cf60 Yarrowia lipolytica (Candida lipolytica) lipolytica .
PPase_methylesterase_euk :
yarli-ppme1 Yarrowia lipolytica (Candida lipolytica) protein phosphatase methylesterase 1 (EC 3.1.1.-) (pme-1) .
Proline_iminopeptidase :
yarli-q6cg13 Yarrowia lipolytica (Candida lipolytica) similar to tr|q96vt2 aspergillus niger prolyl aminopeptidase a .
Steryl_acetyl_hydrolase :
yarli-q6c493 Yarrowia lipolytica (Candida lipolytica) similar to wi|ncu07890.1 neurospora crassa ncu07890.1 Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can
retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Yarrowia lipolytica CLIB122:
N ,
E .
Molecular evidence
Database
No mutation No structure No kinetic No Substrate No inhibitor
Sequence
Graphical view for this peptide sequence: yarli-q6cep3 Colored MSA for Duf_676 (raw)
MHLFVLIHGLWGSATHMAAVKEVLDTTYGVKAGGDMVAYATQSNHGTLTY
DGVQVCARRCYLEIKEVIRRYADDEGVTFDRISILGYSLGGLIARYLCGI
FLDEGFFDKVKPVLFSTIATPHLGSKFHRTDKRWFSWMNTLGSTYLGNTG
RDLFLKDPTLADMSNPSSSAYKALEMFDNRVLLANCRNDRTVHFPTAFIT
AANPFANLRWLDLKFHEVKLQEPVVDSYGWSHSPRIIDFKRTTKRSLPFP
VYHEHIRQKLIFWSFAATVGPLAITAVLIASMFFTNNSNHRVSKFLREGD
KALMGEILESIKMETFDEEWLNEGDERKVGGKGEKTENTDKQSSPVSKTD
ASKVEEEADVMAAGITEAAVEDVILGDDLNNTDTPALSETKVVGLGEAME
AARHTGDRGLLANWANNAPFSEDVLSMIENMDKLGWEKYAVYITVIHSHA
AIVARRGLTQQGQGAATLRLFSEIIRSKI
Legend
This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA
M H L F V L I H G L W G S A T H M A A V K E V L D T T Y G V K A G G D M V A Y A T Q S N H G T L T Y D G V Q V C A R R C Y L E I K E V I R R Y A D D E G V T F D R I S I L G Y S L G G L I A R Y L C G I F L D E G F F D K V K P V L F S T I A T P H L G S K F H R T D K R W F S W M N T L G S T Y L G N T G R D L F L K D P T L A D M S N P S S S A Y K A L E M F D N R V L L A N C R N D R T V H F P T A F I T A A N P F A N L R W L D L K F H E V K L Q E P V V D S Y G W S H S P R I I D F K R T T K R S L P F P V Y H E H I R Q K L I F W S F A A T V G P L A I T A V L I A S M F F T N N S N H R V S K F L R E G D K A L M G E I L E S I K M E T F D E E W L N E G D E R K V G G K G E K T E N T D K Q S S P V S K T D A S K V E E E A D V M A A G I T E A A V E D V I L G D D L N N T D T P A L S E T K V V G L G E A M E A A R H T G D R G L L A N W A N N A P F S E D V L S M I E N M D K L G W E K Y A V Y I T V I H S H A A I V A R R G L T Q Q G Q G A A T L R L F S E I I R S K I
Reference
Title: Genome evolution in yeasts
Dujon B , Sherman D , Fischer G , Durrens P , Casaregola S , Lafontaine I , De Montigny J , Marck C , Neuveglise C and Souciet JL <57 more author(s)>
Dujon B , Sherman D , Fischer G , Durrens P , Casaregola S , Lafontaine I , De Montigny J , Marck C , Neuveglise C , Talla E , Goffard N , Frangeul L , Aigle M , Anthouard V , Babour A , Barbe V , Barnay S , Blanchin S , Beckerich JM , Beyne E , Bleykasten C , Boisrame A , Boyer J , Cattolico L , Confanioleri F , de Daruvar A , Despons L , Fabre E , Fairhead C , Ferry-Dumazet H , Groppi A , Hantraye F , Hennequin C , Jauniaux N , Joyet P , Kachouri R , Kerrest A , Koszul R , Lemaire M , Lesur I , Ma L , Muller H , Nicaud JM , Nikolski M , Oztas S , Ozier-Kalogeropoulos O , Pellenz S , Potier S , Richard GF , Straub ML , Suleau A , Swennen D , Tekaia F , Wesolowski-Louvel M , Westhof E , Wirth B , Zeniou-Meyer M , Zivanovic I , Bolotin-Fukuhara M , Thierry A , Bouchier C , Caudron B , Scarpelli C , Gaillardin C , Weissenbach J , Wincker P , Souciet JL (- 57)
Ref: Nature, 430 :35, 2004 : PubMed Abstract ESTHER: Dujon_2004_Nature_430_35 PubMedSearch: Dujon 2004 Nature 430 35 PubMedID: 15229592 Gene_locus related to this paper: canga-apth1 ,
canga-ppme1 ,
canga-q6fik7 ,
canga-q6fiv5 ,
canga-q6fiw8 ,
canga-q6fj11 ,
canga-q6fjh6 ,
canga-q6fjl0 ,
canga-q6fjr8 ,
canga-q6fkj6 ,
canga-q6fkm9 ,
canga-q6fku7 ,
canga-q6fl14 ,
canga-q6flb5 ,
canga-q6fle9 ,
canga-q6flk8 ,
canga-q6fly1 ,
canga-q6fly9 ,
canga-q6fmz4 ,
canga-q6fnx4 ,
canga-q6fp28 ,
canga-q6fpa8 ,
canga-q6fpi6 ,
canga-q6fpv7 ,
canga-q6fpw6 ,
canga-q6fqj3 ,
canga-q6fr97 ,
canga-q6frt7 ,
canga-q6ftm9 ,
canga-q6ftu0 ,
canga-q6ftv9 ,
canga-q6ftz9 ,
canga-q6fuf8 ,
canga-q6fv41 ,
canga-q6fvu3 ,
canga-q6fw36 ,
canga-q6fw94 ,
canga-q6fwk6 ,
canga-q6fwm0 ,
canga-q6fxc7 ,
canga-q6fxd7 ,
debha-apth1 ,
debha-atg15 ,
debha-b5rtk1 ,
debha-b5rub4 ,
debha-b5rue8 ,
debha-b5rue9 ,
debha-bna7 ,
debha-ppme1 ,
debha-q6bgx3 ,
debha-q6bh69 ,
debha-q6bhb8 ,
debha-q6bhc1 ,
debha-q6bhd0 ,
debha-q6bhj7 ,
debha-q6bi97 ,
debha-q6biq7 ,
debha-q6bj53 ,
debha-q6bkd8 ,
debha-q6bks1 ,
debha-q6bky4 ,
debha-q6bm63 ,
debha-q6bmh3 ,
debha-q6bn89 ,
debha-q6bnj6 ,
debha-q6bp08 ,
debha-q6bpb4 ,
debha-q6bpc0 ,
debha-q6bpc6 ,
debha-q6bq10 ,
debha-q6bq11 ,
debha-q6bqd9 ,
debha-q6bqj6 ,
debha-q6br33 ,
debha-q6br93 ,
debha-q6brg1 ,
debha-q6brw7 ,
debha-q6bs23 ,
debha-q6bsc3 ,
debha-q6bsl8 ,
debha-q6bsx6 ,
debha-q6bta5 ,
debha-q6bty5 ,
debha-q6btz0 ,
debha-q6bu73 ,
debha-q6buk9 ,
debha-q6but7 ,
debha-q6bvc4 ,
debha-q6bvg4 ,
debha-q6bvg8 ,
debha-q6bvp4 ,
debha-q6bw82 ,
debha-q6bxr7 ,
debha-q6bxu9 ,
debha-q6bym5 ,
debha-q6byn7 ,
debha-q6bzj8 ,
debha-q6bzk2 ,
debha-q6bzm5 ,
klula-apth1 ,
klula-ppme1 ,
klula-q6cin9 ,
klula-q6ciu6 ,
klula-q6cj47 ,
klula-q6cjc8 ,
klula-q6cjq9 ,
klula-q6cjs1 ,
klula-q6cjv9 ,
klula-q6ckd7 ,
klula-q6ckk4 ,
klula-q6ckx4 ,
klula-q6cl20 ,
klula-q6clm1 ,
klula-q6cly8 ,
klula-q6clz7 ,
klula-q6cm48 ,
klula-q6cm49 ,
klula-q6cmt5 ,
klula-q6cn71 ,
klula-q6cnm1 ,
klula-q6cr74 ,
klula-q6cr90 ,
klula-q6crs0 ,
klula-q6crv8 ,
klula-q6crz9 ,
klula-q6cst8 ,
klula-q6csv8 ,
klula-q6ctp8 ,
klula-q6cu02 ,
klula-q6cu78 ,
klula-q6cu79 ,
klula-q6cuv3 ,
klula-q6cvd3 ,
klula-q6cw70 ,
klula-q6cw92 ,
klula-q6cwu7 ,
klula-q6cx84 ,
klula-q6cxa3 ,
klula-q6cy41 ,
yarli-apth1 ,
yarli-atg15 ,
yarli-BST1B ,
yarli-lip2 ,
yarli-LIP3 ,
yarli-LIP4 ,
yarli-LIP5 ,
yarli-LIP7 ,
yarli-LIP8 ,
yarli-lipa1 ,
yarli-ppme1 ,
yarli-q6bzp1 ,
yarli-q6bzv7 ,
yarli-q6c1f5 ,
yarli-q6c1f7 ,
yarli-q6c1r3 ,
yarli-q6c2z2 ,
yarli-q6c3h1 ,
yarli-q6c3i6 ,
yarli-q6c3l1 ,
yarli-q6c3u6 ,
yarli-q6c4h8 ,
yarli-q6c5j1 ,
yarli-q6c5m4 ,
yarli-q6c6m4 ,
yarli-q6c6p7 ,
yarli-q6c6v2 ,
yarli-q6c7h3 ,
yarli-q6c7i7 ,
yarli-q6c7j5 ,
yarli-q6c7y6 ,
yarli-q6c8m4 ,
yarli-q6c8q4 ,
yarli-q6c8u4 ,
yarli-q6c8y2 ,
yarli-q6c9r0 ,
yarli-q6c9r1 ,
yarli-q6c9u0 ,
yarli-q6c9v4 ,
yarli-q6c209 ,
yarli-q6c225 ,
yarli-q6c493 ,
yarli-q6c598 ,
yarli-q6c687 ,
yarli-q6c822 ,
yarli-q6cau6 ,
yarli-q6cax2 ,
yarli-q6caz1 ,
yarli-q6cb63 ,
yarli-q6cba7 ,
yarli-q6cbb1 ,
yarli-q6cbe6 ,
yarli-q6cby1 ,
yarli-q6ccr0 ,
yarli-q6cdg1 ,
yarli-q6cdi6 ,
yarli-q6cdv9 ,
yarli-q6ce37 ,
yarli-q6ceg0 ,
yarli-q6cep3 ,
yarli-q6cey5 ,
yarli-q6cf60 ,
yarli-q6cfp3 ,
yarli-q6cfx2 ,
yarli-q6cg13 ,
yarli-q6cg27 ,
yarli-q6cgj3 ,
yarli-q6chb8 ,
yarli-q6ci59 ,
yarli-q6c748 ,
canga-q6fpj0 ,
klula-q6cp11 ,
yarli-q6c4p0 ,
debha-q6btp5 ,
debha-kex1 Abstract
Identifying the mechanisms of eukaryotic genome evolution by comparative genomics is often complicated by the multiplicity of events that have taken place throughout the history of individual lineages, leaving only distorted and superimposed traces in the genome of each living organism. The hemiascomycete yeasts, with their compact genomes, similar lifestyle and distinct sexual and physiological properties, provide a unique opportunity to explore such mechanisms. We present here the complete, assembled genome sequences of four yeast species, selected to represent a broad evolutionary range within a single eukaryotic phylum, that after analysis proved to be molecularly as diverse as the entire phylum of chordates. A total of approximately 24,200 novel genes were identified, the translation products of which were classified together with Saccharomyces cerevisiae proteins into about 4,700 families, forming the basis for interspecific comparisons. Analysis of chromosome maps and genome redundancies reveal that the different yeast lineages have evolved through a marked interplay between several distinct molecular mechanisms, including tandem gene repeat formation, segmental duplication, a massive genome duplication and extensive gene loss.
         Other Papers