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Database: UniProt
Entry: F4PFF6_BATDJ
LinkDB: F4PFF6_BATDJ
Original site: F4PFF6_BATDJ 
ID   F4PFF6_BATDJ            Unreviewed;       472 AA.
AC   F4PFF6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGF76038.1};
GN   ORFNames=BATDEDRAFT_18145 {ECO:0000313|EMBL:EGF76038.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog
OS   chytrid fungus).
OC   Eukaryota; Fungi; Chytridiomycota; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF76038.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-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; GL882927; EGF76038.1; -; Genomic_DNA.
DR   RefSeq; XP_006683342.1; XM_006683279.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EGF76038; EGF76038; BATDEDRAFT_18145.
DR   GeneID; 18237255; -.
DR   InParanoid; F4PFF6; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
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:UP000007241};
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:UP000007241};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   472 AA;  51437 MW;  A9FDDAB92C18E912 CRC64;
     MNLAKDFLKF VDASPSPFHA VESCIARLVK AGFTELKEGD AWTTSTVLAN GKYFFSRNKS
     AIIAFCVGGK YSPTSGFSII GAHTDSPCLK IKPRSKREKA GCIQVGVELY GGGLWHTWFD
     RDLSVAGRVL VATKNTQGVE SFTHALAKID KPLLRIPTLA IHLDRSANDG FNFNKEVQLT
     PILGIAQKIL EKKDDTNDVG TLHHPMLLKE VATNLGVQAE SIRDFELCLY DTQPSSIGGA
     NNEFIHSARL DNLMMSFCAL TAIIESANTL DQDSKIRVVG LFDNEEVGSQ TAHGANSNFM
     QTTLQRLSDM DIGGSSQVLA GARYERSMVN SLLISADMAH ALHPNYFEKH EDNHRPLINS
     GVVIKQNANQ RYATTAISTL VLREVAKLAG KEGSGGVALQ EFVVRNDSPC GSTIGPMLSA
     SLGVRTVDVG NPQWSMHSIR ETCGVEDVQH AVNLFKSFFD HFAAVDARIP RL
//
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