ID A0A150VAD4_9PEZI Unreviewed; 772 AA.
AC A0A150VAD4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_152224 {ECO:0000313|EMBL:KYG47469.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47469.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG47469.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG47469.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG47469.1}.
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DR EMBL; JPDO01000077; KYG47469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VAD4; -.
DR STRING; 766039.A0A150VAD4; -.
DR Proteomes; UP000075602; 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:UP000075602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 772 AA; 85094 MW; 0F7844540604568E CRC64;
MVRNAVSMQN LYTKANVNTD ESCPNVQTIF RPSSSMLNRL PQADIEQQHH VRFNQPIQLH
GNDDYTKWLM TRIATGQATT EEKAKWNEHV AIIKGQSTER NAVPSPTPIG WVSPEPTADL
TARGIQQIED GNSQAHADYH LQLKLLEWQS KQRLRMVRNT EGLGRSSMPL QGSNSNISGE
YEYEEAETKQ KKDIINNTRK NNTATVNVKS PGIADATQGR RFLLAQKEIE ELGNRWATDH
NPLLSKPEDE YTMEDNAEID RLWKAHLAQR SSQKQYSRRQ GKKIEQERFK QATRDNAAKY
AKPFCDFMTN NPTVFHAVDA IKFQLKGCGF KELSERDSWD LEAGASYFVE RNGSSLMAFT
IGSKYTPGNG AAILAGHVDA LCAKLKPMSE VPNKAGYLQL GVAPYAGAPN MTWWDRDLSI
GGRVLVKDGD RIITKLVKLD WPIARIPTLA PHFGAASQPP FNPETQMVPI IGLESTNSRD
VENEPFSQPS IVGFSGAFPY TSTWICKQPP KLVKAIGDAI GLTAGTYSKI LNWELELYDT
QPATLGGLDK EFIFAGRIDD KLCSWAAIQA LIEAGQSGDT EESSLIKLVG LFDDEEIGSG
LRQGARSNFL PLVLERIVGS FSDGKSSASE LMGRTYANSF LLSSDVIHAV NPNFLDSYLE
NHSPHLNVGL AISADPNGHM TTDSSSIAVL QRCADKIGAK LQVFQIRNDS RSGGTVGPVL
SSMTGIRAID AGIPQLSMHS IRATTGSLDP GLGVLMFRGF LNGFESVDKE FR
//
