ID U7PZJ4_SPOS1 Unreviewed; 607 AA.
AC U7PZJ4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Vacuolar aminopeptidase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_02254 {ECO:0000313|EMBL:ERT01018.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT01018.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290}.
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DR EMBL; KI440843; ERT01018.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PZJ4; -.
DR STRING; 1391915.U7PZJ4; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_3_0_1; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000018087; 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF4; VACUOLAR AMINOPEPTIDASE 1; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 64403 MW; 3BBD51B037C52F33 CRC64;
MARREAPTEI PLRYNTLRQA TSHRERLNQR FASGSYSTLN AAMASPSVAS SSPSVSSSSA
SSTPASSPPL AAATPATRSI ESQCYIQSGM ADRTPAENTI CVSCARSLHD VDVSTCRVTQ
NSETHCVICA WKRGDAATFT KPFLRFITEN PTVFHAVGYF EKQLADAGFV KLSARDDWSG
TIQPGGKYYV TRNGSSLIAF TVGGAYVPGN GVAIVAGHID ALTARLKPVS SKPTKVGYQQ
LGVAPYAGAL NATWWDRDLA IGGRVVVRDP STSKVSTRLV KLGWPIAKIA TLAPHFGVSM
TGSGNKETQM VPIIGLDDTD GAGGAGEAIA GANAFVAQQP PKLVKLIAAE LGIDDYSLIL
NWELELYDHQ PATVLGVDRD LISAGRIDDK ICSWAALVAL LRAQDNDDAG VIRLAAFFDD
EEIGSLLRQG AWGNFLPVTI ERAVESLAAN KNAGSGAAAA LGPGLVARTY AASFLVSADV
THAVHPNFVG NYLDDHQPRL NVGITVAYDS NGHMTTDSVS TAILTRVAEL SGNTLQRFMI
RNDSRSGGTI GPELSSMIGV RSIDAGIPQL SMHSIRATTG ALDPGLGVKL FQSFFELYEK
VDAEWQE
//
