ID   A0A2K5ANP0_9ARCH        Unreviewed;       837 AA.
AC   A0A2K5ANP0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative membrane alanyl aminopeptidase {ECO:0000313|EMBL:SPC33219.1};
DE            EC=3.4.11.2 {ECO:0000313|EMBL:SPC33219.1};
GN   ORFNames=NCAV_0019 {ECO:0000313|EMBL:SPC33219.1};
OS   Candidatus Nitrosocaldus cavascurensis.
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Candidatus Nitrosocaldales;
OC   Candidatus Nitrosocaldaceae; Candidatus Nitrosocaldus.
OX   NCBI_TaxID=2058097 {ECO:0000313|EMBL:SPC33219.1, ECO:0000313|Proteomes:UP000236248};
RN   [1] {ECO:0000313|Proteomes:UP000236248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCU2 {ECO:0000313|Proteomes:UP000236248};
RA   Kerou L M.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; LT981265; SPC33219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K5ANP0; -.
DR   KEGG; ncv:NCAV_0019; -.
DR   Proteomes; UP000236248; Chromosome ncav.
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; 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; 3.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM00567; EZ_HEAT; 7.
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:SPC33219.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SPC33219.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          30..201
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          237..445
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   COILED          806..833
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   837 AA;  97136 MW;  309D5914317AEA53 CRC64;
     MNRVANNSKR FELPGSKAHY APSKPFLIKH IRLELKPDLN EGSINAREDI EITANSEKVR
     SIVLDAAELK IARVMLGEQE LNFKHVDERL RIELPRELKE GENVKITIEY SAKPRKGLHF
     IKPDEHYPKR RLQAWTQGES IYSKYWFVCI DHPDIRFTSE MIVDVPDGFT AVSNGRLVRV
     EDNGSYKRYH WLEECGHPAY LTSLAIGRFR ELRDEYNGVE LLYYVPEDMV DYAELSFANT
     KDMMRFFEEY TGVKYPYSKY AQVTVDDFIY GGMENINATT LTVETLHDKR AHIDFTSDHL
     VAHELAHQWF GDLVTCRDWQ HIWLNESFAT YFEALYWLHS RGEDEFNYYI MQYANEYFEE
     YSKRYARPIV TNVYKHPDDL FDRHAYEKGA CVLHMLRCMI GDKQFRRAIK HYLERFRLSN
     AESEEFRRCC EDATGYSLQE FFEQWLYRAG HPELKIKVDY NHDTSMLNIN IAQVQSIDEG
     KPFIFPLDVH IVSRDGKREE IMLNIEAKEQ SMHIPLKYEP MYISIDPLNK LPLKKIVELK
     IDKHMLIAML KHGNTVERIN AARALANTTM DSDDVINALR EAIVSDAFWG VAAEAAKALA
     SIKGEKAYSA LTSIVESIKH PKARRAVVRA IGEFAREDSI QLLNRIVQSD ESYYVQAEAV
     LAIGKSKSKK ALPYLMGSLQ IRSHNEVVRA SAMAAFGEVR DEFSIPVLID HTRLGEHNRV
     REAATLALSK YAKGNEKVVD HLIQLLRDHW FRVRINAIKA LAEAQEQKAL RDLEWVASND
     IDARVRRVAE EAIITIREAT QVPKELAQMR EEVERLKGMS RDMMSRLDML EREIKSS
//