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Database: UniProt
Entry: G3B675_CANTC
LinkDB: G3B675_CANTC
Original site: G3B675_CANTC 
ID   G3B675_CANTC            Unreviewed;       537 AA.
AC   G3B675;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   28-FEB-2018, entry version 28.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGV63402.1};
GN   ORFNames=CANTEDRAFT_114712 {ECO:0000313|EMBL:EGV63402.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 /
OS   NBRC 10315 / NRRL Y-1498 / VKM Y-70) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Yamadazyma;
OC   Yamadazyma/Candida clade.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV63402.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A.,
RA   LaButti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A.,
RA   Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E.,
RA   Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL996524; EGV63402.1; -; Genomic_DNA.
DR   RefSeq; XP_006687195.1; XM_006687132.1.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EGV63402; EGV63402; CANTEDRAFT_114712.
DR   GeneID; 18247546; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000707};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    537       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003442742.
SQ   SEQUENCE   537 AA;  59319 MW;  C133CF7B7334DAA8 CRC64;
     MWITLFLVLY LPNALWSCGF LQLRAGLSRK TTYPFNSYLM PETYAFIDAE DILSWDELST
     DDEHPVIAPV QSSSQNSPST STCHKYLEFT DMNPTTFHVV RHFAKLLDDN GFVFIDEQEP
     ITPELEAQIN AGGKFYTLRS DLTILPFVIG GKWTATQGVG LAGCHIDALT AKLKPSSLKP
     KVDGYELLGV TGYSGGLDHL RLDRDLGLGG AVLIRRKDGT YARKLVTSPW PIARVPSLAE
     HFGVDAKYNP ETEMVPVIGF DTEPEVPIDH PLADRHSAKL LRYVSSISDV PVDDIVELEL
     ELYDTQKAVI GGLKGEFVFA PRLDDRLCSW AAIYGLIEYA NLYDSDSLAA HDGLSMVLLV
     DSEEIGSGTR TGVKGKFLNA TIDKILVIKK QPPVQSVVFA NSILLSADVT HLMNPNFKSA
     YLDKHYPLPN TGMTIKIDAN GHVASEYVGY NLLKTLTSQN QLKLQQFHIR NDASSGGTIG
     PYLATATGAR VIDIGLPILS MHSVRAMCGS EDVQNGVDFF KAFFEGWRQE YNKYRGL
//
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