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Database: UniProt
Entry: Q8ZWW0_PYRAE
LinkDB: Q8ZWW0_PYRAE
Original site: Q8ZWW0_PYRAE 
ID   Q8ZWW0_PYRAE            Unreviewed;       822 AA.
AC   Q8ZWW0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:AAL63589.1};
GN   OrderedLocusNames=PAE1597 {ECO:0000313|EMBL:AAL63589.1};
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL63589.1, ECO:0000313|Proteomes:UP000002439};
RN   [1] {ECO:0000313|EMBL:AAL63589.1, ECO:0000313|Proteomes:UP000002439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC   IM2 {ECO:0000313|Proteomes:UP000002439};
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; AE009441; AAL63589.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZWW0; -.
DR   STRING; 178306.PAE1597; -.
DR   EnsemblBacteria; AAL63589; AAL63589; PAE1597.
DR   KEGG; pai:PAE1597; -.
DR   PATRIC; fig|178306.9.peg.1178; -.
DR   eggNOG; arCOG02969; Archaea.
DR   HOGENOM; CLU_014298_0_1_2; -.
DR   InParanoid; Q8ZWW0; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF13646; HEAT_2; 2.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; ARM repeat; 1.
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:0000313|EMBL:AAL63589.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002439};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          30..188
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          223..443
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   COILED          789..820
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   822 AA;  95709 MW;  54B2A2781BBB4913 CRC64;
     MAMRYLVGRD FAFPEYLPRF PPEYHFEVSH MQLDITIDVE GGWVEGVVRY RAKAKKDRAA
     VVLDAMEMEI LEASHEYFYD GSKVEIKPEW KRGDPVEIYV KYRTRPRAGM YFIKTGKGYY
     VWTQGESEYN RYWVPLPDSP NIKFPWTVAI TVPKPYIAGS NGVLIEVKDR GERQTFVWDL
     KHPMSPYLLA IAVGDFEIHR EKCGDVVLEF YIPRYVDDRW RFSFYNTCRI MQFFSEYLGV
     PFPYERYAQV VVPEFIYGGM ENTTFTILTD WTIHDKHAHC PYTGFPCPER EDFSSDPLVA
     HEMAHMWFGD LVTAKDWAHI AINESFATFI EALWTEAHKG REEYLYEIYT NFKTYLGEFS
     RRYSRPIVTN LYKIPDEVFD RHAYEKGSVV LHTLRSILGD DVFRKALKLF LERHRYKAVD
     FEDLRKAFEE TAGRDLEWFW RQFWYSAGHP VLKVSWSYSE GAIKLQIKQA QGEDSYPVYT
     LPLEIKIVYE DGRREVKEVF LNMKEVTLYI EGGKPKYICV DPSFKIIKAL DLQYPLESAV
     AMIDDDDMYC KIQAIEVLKK NGSPRAVNAL AKAVGDKFWG VAAEAARALG EIGTEEAMAK
     LTEAFKKSLH PRVRRVIVEA LGNTKRKEAG EFLDKILHDA GESYYVRAEA ARALGKVKWE
     FAEFSLKKAL EYPSHLDVIK RGALEGLAEL GTEEALKIVL RHAEPGMPTP VRVSAVQSLA
     KFGPRKEVID ALKRYMRDDN FRMRYAAVTA ALELLEPRLL QDLQERAEQD IDGRIRRVAR
     EIVEKIKKSM ERGAEYQKLR EEVEKLREEY RKLLDRIARL EK
//
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