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Database: UniProt
Entry: C5FTY4_ARTOC
LinkDB: C5FTY4_ARTOC
Original site: C5FTY4_ARTOC 
ID   C5FTY4_ARTOC            Unreviewed;       492 AA.
AC   C5FTY4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EEQ33368.1};
GN   ORFNames=MCYG_06187 {ECO:0000313|EMBL:EEQ33368.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum
OS   canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33368.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mBio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T.,
RA   Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A.,
RA   White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; DS995706; EEQ33368.1; -; Genomic_DNA.
DR   RefSeq; XP_002844223.1; XM_002844177.1.
DR   ProteinModelPortal; C5FTY4; -.
DR   STRING; 554155.XP_002844223.1; -.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EEQ33368; EEQ33368; MCYG_06187.
DR   GeneID; 9222462; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000002035; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EEQ33368.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002035};
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:UP000002035};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   492 AA;  53623 MW;  5A51B2FF7BAC682A CRC64;
     MITADEKARA NDFLSFVNAS PTPFHAVASA TKRFTDAGFK EIKEKDCWSD VCKPGGKYYV
     TRNGSTIIAF AVGNKWKPGN SIAMIGAHTD SPCLRIKPVS KRTNEGFLQI AVEPYGGGIW
     HTWFDRDLGI AGRVMVRQQD GTIASKLVHI DKPILRIPTL AIHLDRTETF AFNKETQLVP
     ICGMVAAELS KTNDSPKPED SGDSVSPFKK ITERHHPCLI ELLASELSAK PDDIIDFEML
     LYDTHKSCLG GMMDQFIFSP RLDNLNSSFC ATVALVESLA KPSALENETA IRLVALFDHE
     EIGSRTAQGA DSNILPAIIH RLSMLRVSGS NSDEDLSTAY EQSLSTSFLV SADMAHAVNP
     NYAYKYESEH KPEINRGPVI KVNANARYAT NTPGIVLMHE VARAAVAKSD ISSDSIVPMQ
     LLVVRNDSSC GSTIGPMLSA ALGSRTLDLG SPQLSMHSIR ETGGTKDVAL ATRLFTSFFE
     NYTALAPKIL ID
//
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