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Database: UniProt
Entry: A0A0L0HQM4_SPIPN
LinkDB: A0A0L0HQM4_SPIPN
Original site: A0A0L0HQM4_SPIPN 
ID   A0A0L0HQM4_SPIPN        Unreviewed;       500 AA.
AC   A0A0L0HQM4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KND03691.1};
GN   ORFNames=SPPG_01157 {ECO:0000313|EMBL:KND03691.1};
OS   Spizellomyces punctatus DAOM BR117.
OC   Eukaryota; Fungi; Chytridiomycota; Chytridiomycetes;
OC   Spizellomycetales; Spizellomycetaceae; Spizellomyces.
OX   NCBI_TaxID=645134 {ECO:0000313|EMBL:KND03691.1, ECO:0000313|Proteomes:UP000053201};
RN   [1] {ECO:0000313|EMBL:KND03691.1, ECO:0000313|Proteomes:UP000053201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM BR117 {ECO:0000313|EMBL:KND03691.1,
RC   ECO:0000313|Proteomes:UP000053201};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Thomson T., Walk T., White J., Yandava C., Burger G.,
RA   Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL   Submitted (AUG-2009) 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; KQ257451; KND03691.1; -; Genomic_DNA.
DR   RefSeq; XP_016611730.1; XM_016749481.1.
DR   EnsemblFungi; KND03691; KND03691; SPPG_01157.
DR   GeneID; 27684841; -.
DR   Proteomes; UP000053201; 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; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053201};
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:UP000053201};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   500 AA;  55190 MW;  FF7E73E238CEC81E CRC64;
     MRFLTYGRPS TCLLHTSHRP TVHFTTSTPS TLATQSASDF IDFVNSSPSP FHAVETSRQR
     LLAAGFEEIR ERDTWSGKLR REGKYFFTRN KSSITAFAVG GKYVSGNGFS VVGAHTDSPC
     LKVKPHSKKE KGGYTQVGVQ LYGGGLWHTW FDRDLGIAGR VLVRTAEGKL DHRLVRVDRP
     ILRIPTLAIH LDRGVSEGFK FNNEVQLTPI LASAATKMLN ADAEQKNAVH QAPNEDKHAP
     LLLKILADEL KLDGDQLGDF ELCLYDTQPS TIGGAQNEYI FSARLDNLMM SYCSITALVN
     STKGDSLQKD PNIRVVVLFD NEEVGSVSSY GAGSNLLEIT LRRLAAEVET GDKAESSFER
     AMTRSLLISA DMAHALHPNY LEKHEENHRP AMNKGVVIKQ NANQRYATTA VSTAIVREVA
     RKRNVPLQEF VVRNDSPCGS TIGPMLSAKL GLRTIDVGNP QLSMHSIRET AGVEDVKHAV
     ALFESFFEEF AVVDEQVFVD
//
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