ID A0A1Q7M7T0_9CREN Unreviewed; 796 AA.
AC A0A1Q7M7T0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=AUI95_02455 {ECO:0000313|EMBL:OLD08718.1};
OS Crenarchaeota archaeon 13_1_40CM_3_52_4.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805097 {ECO:0000313|EMBL:OLD08718.1, ECO:0000313|Proteomes:UP000186346};
RN [1] {ECO:0000313|EMBL:OLD08718.1, ECO:0000313|Proteomes:UP000186346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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}.
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:OLD08718.1}.
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DR EMBL; MNGM01000037; OLD08718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7M7T0; -.
DR Proteomes; UP000186346; 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; 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:0000256|RuleBase:RU364040};
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 4..165
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 199..415
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 484..773
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 356
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 796 AA; 90723 MW; BE3FE18A69CC224A CRC64;
MQIESYDLFL NVDFRNLRFD GKVKIKLESE TDVKLNSVEL EILEVDANGK PVKYNLEGED
FTIKTGKFVG ELGIRYRGSI SDKLVGLYKA AYEGGYVVST QFEAVSARRL LPCMDHPAYK
ADFKLTIRTD SDTSVISNMP STSVRVDGPR KTVEFPKTPR MSTYLMYLGI GKFEEVKDRF
NGVDYIVATV PGKSSGAKFP LDVAKDSVRF FESYFGSKYN LPKLHLIGVP EFAAGAMENW
GAITFREIAL LVDDDSSIRI RKQVAEVIAH EVSHQWFGDL VTMKWWDDLW LNESFATFMA
YKALDSMFPR WVVWQDFVRG ETAGALARDS LVNTHPIEVR VNSPTEIEEI FDDISYGKGA
SIIRMLEAYA GEDEFMHGVR SYLEKYKFSN AAGNDLWNEI ERTSKTRVKA IMNDWIRKPG
YPVVNVKLDG KKLMIRQHRF LLNGSAEPSS WPVPITLKIN GKEQKLLMEK SEESIAVPDG
VDSLKLNLEE TGFYRVYYEG LYDKVWRSNM SPVDRYGVVS DAYAFAIQGK MDFSRYLALI
NRYMNEQEYL PAFEVSDQLS SLSTITRSVE ETSRKFHRNQ LKILANRKDE NSVALQGSVA
SRLALLDMEY AKELSLRFND YETAEPDMKQ AIVVAHARAS GDFESLFKNY KNRPSEEEKS
RFLIGLTSFN QPSLNSRAMD LASSGEIRKQ HVGTLLGSAA RNPDARDGTW DWIAQKFEWL
RGIYEGTGVL SRYLTYVLPI LGIDRTEEVT KFFAKHKAPE IIKGVEAGLE KLRINEAFLR
RIGPSQKQMV EVQERR
//
