ID B8MIM0_TALSN Unreviewed; 877 AA.
AC B8MIM0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 08-NOV-2023, entry version 64.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=TSTA_045700 {ECO:0000313|EMBL:EED15112.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED15112.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; EQ962657; EED15112.1; -; Genomic_DNA.
DR RefSeq; XP_002485065.1; XM_002485020.1.
DR AlphaFoldDB; B8MIM0; -.
DR STRING; 441959.B8MIM0; -.
DR MEROPS; M01.A25; -.
DR GeneID; 8107557; -.
DR VEuPathDB; FungiDB:TSTA_045700; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; B8MIM0; -.
DR OMA; NVWSQFV; -.
DR OrthoDB; 3085317at2759; -.
DR PhylomeDB; B8MIM0; -.
DR Proteomes; UP000001745; 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:UniProtKB-UniRule.
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:SF171; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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|RuleBase:RU364040,
KW ECO:0000313|EMBL:EED15112.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 15..208
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 248..465
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 539..854
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 406
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 877 AA; 98121 MW; A7F95F7B4645C4B8 CRC64;
MARSDRDTLP DVVKPKRYDI SLYNLQLGGS WGYNGTVKID VKASKPTKEI VLNTKEVSVE
KAEVQAGSTS VKAVGISYDK VSERVTLAFD QEIPSGEALL KIDFTATINE AMAGFSRCKY
KAPVTPSAAT PESDGYHYMM STQFEACDAR RAFPCFDEPN LKAEFDFEIE VPKDLVALSN
MPVKSERDSK EGWKVVSFER TPIMSTYLLA WAVGDFGYVE AKTERKYNGA SIPVRVYTTR
GLEDQARYAL ECAHKTVDYF SELFGIEYPL PKSDLLCVHA FAAGAMENWG LVTYRTTAVL
FDEGKSDSRY KNRIAYVVAH ELAHQWFGNL VTMDWWSELW LNEGFATWVG WLAVDHFHPD
WNVWSQFVAE GVQQASQLDS LRASHPIEVP VKNALEVDQI FDHISYLKGS SVIRMLSSHL
GQDVFINGVS NYLKTHAYGN ATTNDLWLAL SKASNLDVNA LMNPWIRKIG YPVVTVAEEP
GQISLRQNRF LSSGDVKPEE DETVWWIPLG IKSGAQPTQV KLDALTSKSD TFRGINEEFY
KINKDHSGFY RTNYPPQRLA KLGQSLHLLS TEDKIGLVGD AAALAVSGES TTPALLALIE
GFAQEANYLV WSQTSSSLAS LRTTFSSNES AAAAIKKFKL KLVTPAVEKI GWEFRSDEDY
LTGQLRKLLI AMAGEAGHEG IVAEAKRRFQ LWASGQDPNA IHSNLRSTIF SINVAEGDRA
EFERIKEEFV QTDSVDGKEI CLSALGRAKN PELIQEYLNF IFSDKVSIQD VHTGAASLAN
NPIGRYALWE YMKSNWTAVS TRLSANNIVY DRFVRLGLSK FSEVAIADDI AKFFEDKDTG
AFERTLVILS DSIRTNARYK ERDEKLLLEW MQAHGYA
//
