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Database: UniProt
Entry: A0A0D2JLC5_9EURO
LinkDB: A0A0D2JLC5_9EURO
Original site: A0A0D2JLC5_9EURO 
ID   A0A0D2JLC5_9EURO        Unreviewed;       507 AA.
AC   A0A0D2JLC5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-NOV-2017, entry version 14.
DE   SubName: Full=Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.1, whole genome shotgun sequence {ECO:0000313|EMBL:KIX10260.1};
GN   ORFNames=Z518_01341 {ECO:0000313|EMBL:KIX10260.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX10260.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX10260.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX10260.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KN847475; KIX10260.1; -; Genomic_DNA.
DR   RefSeq; XP_013277396.1; XM_013421942.1.
DR   EnsemblFungi; KIX10260; KIX10260; Z518_01341.
DR   GeneID; 25289412; -.
DR   Proteomes; UP000053617; 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   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053617};
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:UP000053617};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   507 AA;  55353 MW;  3E0AE3388170E99A CRC64;
     MPPVDVKVAA HDFLDFVNAS PTPFHAVKSV KERLSKVGFQ EIKEKESWSS TCLPGGKYFL
     TRNGSTIVAF AIGNKWKPGN PISMVGAHTD SPCLRIKPVS KKQGDGFLQV GVETYGGGLW
     HTWFDRDLGI AGRAMVRGAD GNVVQKLVHI TKPILRVPTL AVHLDRQETF SFNKETQLFP
     IAGLVAAELN RQGKKKDPTS SEEEEQARPF TPLKAMTTRH HPHIVELIAK DAGVSPEDVV
     DFEMVLYDTQ KACLGGLTDE FIFSARLDNL NQTYCATMGL IHSLRSSSAL DDESSIRLIA
     CFDHEEIGSM TAQGAFSAML PAVVRRLSVL PSSSFVEETS EESYDHASDP ELSTAYEQTL
     SGSFLLSADM AHSVNPNYGG KYESDHRPEM NQGPVIKINA NAKYATNSPG IVLLQEVARK
     AAKVIDSDPD GVPLQLFVVR NDSSCGTTIG PMLSAHLGAR TLDLGNPQLS MHSCRETGGA
     DDVHHAIRLF SSFFQHYSAL EKTILVD
//
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