ID A0A225ALV1_9EURO Unreviewed; 1002 AA.
AC A0A225ALV1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminopeptidase 2 {ECO:0000313|EMBL:OKL56539.1};
GN ORFNames=UA08_08288 {ECO:0000313|EMBL:OKL56539.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL56539.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL56539.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL56539.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:OKL56539.1}.
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DR EMBL; LFMY01000014; OKL56539.1; -; Genomic_DNA.
DR RefSeq; XP_020116660.1; XM_020263195.1.
DR AlphaFoldDB; A0A225ALV1; -.
DR STRING; 1441469.A0A225ALV1; -.
DR GeneID; 31008044; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000214365; 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; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:OKL56539.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 127..330
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 365..582
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 656..974
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 58..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 523
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1002 AA; 111713 MW; 413EA367D03C37B3 CRC64;
MHPLVSLSSV LPRVCWHSAK PNVLATTRTT TTTQSRLIRN SNLLRTFSAA AAIASTRSSP
PPFRIAPTTT TRTSLRPTAT SSSTTAPLAQ ISKRHCSYRR MCHSRRTDEA LGSTLAQGRE
VLPTNVKPVH YDLTLEPDFE KFTYEGTVVI EHVANWVNSL SPTSLNVNED TNSVSLNTSE
LEIHTSEIIV DGAVVTSSPS VSYDKDKQVT TVNFVETIPA GSKAQLKQTF SGILNDNMAG
FYRSSYKTAD GGTGYIASTQ MEPTDARRAF PCFDEPALKA EFTITLIADK HLTCLSNMDV
ASESEVTSKV SGGTKKAVKF NKSPVMSTYL VAFIVGELKV IESNDFRVPV RVYATLDQDI
EHGRFSLDLA AKTLAFYEKA FDSEYPLPKM DMVAIPDFSA GAMENWGLIT YRVVDLLLDE
KTSGASVKER VAEVVQHELA HQWFGNLVTM DFWDGLWLNE GFATWMSWYS CNIFYPEWKV
WQTYVIDNLQ SALSLDSLRS SHPIEVPVKR ADEVNQIFDA ISYSKGSSVL RMISKYLGED
TFLQGVRDYI RKHAYGNTQT GDLWAALAKA SGKPVEEVMD VWTKYVGFPV VQVTENPSKG
TVNLKQNRFL RTGDVKPEED ETIYPVFLAL RTKDGVHDEL VLDKRENEFK VPDLDFFKVN
ADHSGLYRTS YTPERLEKLG NAAKAGLLTV EDRAGMVADS GALAAAGYQK TSGLLSLLKG
FDTETEFIVW NEMLTRVGSV RAAWLFEDQK TRDSLKAFQR ALVSEKAHQV GWEFSDSDDH
VLQQFKAMLF GSAGAAGDSK VVAAAQDMFK RFLEGDRTAI HPNIRGSVYN IVLKNGGEKE
YNAILEIFRT ASTSDEKNTA LRSLGAAEDI ALVRRTLELA TNGEVRNQDV YMPLSGLRNH
VTGVEERWKW LLENWDAIVA RFPPSLGMLG TIIQLSAVAF NTEEQLKEVE AFFAPKDTKG
FDRAVGQSLD AIRAKAHWLK RDREDVEQWL KTNGYFDVEQ KL
//
