ID   A0A368JR71_9BACT        Unreviewed;       851 AA.
AC   A0A368JR71;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=DUE52_10230 {ECO:0000313|EMBL:RCR69835.1};
OS   Larkinella punicea.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Larkinella.
OX   NCBI_TaxID=2315727 {ECO:0000313|EMBL:RCR69835.1, ECO:0000313|Proteomes:UP000253383};
RN   [1] {ECO:0000313|EMBL:RCR69835.1, ECO:0000313|Proteomes:UP000253383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zzj9 {ECO:0000313|Proteomes:UP000253383};
RA   Zhou Z., Wang G.;
RT   "Genome analysis of Larkinella rosea.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000098};
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}.
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:RCR69835.1}.
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DR   EMBL; QOWE01000007; RCR69835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368JR71; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000253383; 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; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
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; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
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   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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          55..250
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          295..499
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   851 AA;  98281 MW;  4F663286FE199EB1 CRC64;
     MLKIIRNIGF VLLIFISSPW ALGQNRAGDA DKKNAPLTVN GPYNATRTLP HDLLHTKLDL
     SFDWVRQWVH GIARLRFKPH FYPQNTLDVD AKGFEIKGVF LLDTLKTGET VFDTLNYTYN
     DRQKIHVLLP RTYTRADTFD IQIVYTAKPN ERPLGGSAAI SQDKGLYFIN HDGAEPNKPR
     QIWTQGETEA NSCWFPTIDT PNEKMTQEIY LTVENKYRTL SNGKLISSTV NQDSSRTDYW
     RQTLPHSPYL AMIAVGDFAY VKDSLAATPE RGPLEVSYYV EPAYEKDARA IFGRTPAMIE
     FFEKKFGVPY VWEKYSQIAV RDFVTGAMEN TTATVHGETV QMDGRQLVDG NSDDVISHEL
     SHHWFGNLTT AESWANLPLN EAFATYAEYL WREHNEGTYS ADMHGLDDLN QYIAESETKQ
     EPLIRYRYTD REQMFDSHSY AKGGRVLHLL RRTIGDDAFF ESLTLYLKRH RFKTAEISDL
     REVFEEVTGE DLNWFFDQWF LKPGHPVIKI EKEYRQGGVQ LTVIQQQDST KTPIYRLPVK
     VDLWVKGQKK SYDVVVDKAK QVLNFTVEQR PDLIVFDADH RIVGTVEQEK NKPELLFQFY
     HTDNYRDKYE SITRLEDKSN LIDSTVRHMM MDAMQDKFWK IRQVAVGNFA EYDGQEFAEV
     ERIVQSKARN DERSLVRQEG INTLASYADN VNDPLFREAL NDTSYAVVSS ALDSYLLSKP
     GDANEIAARF ENVPNGDIVT AVANYYANST DTSRYTWFIN KMSTMKSQDL YNFLQVFGKY
     LIRSGSDTQR QAIPMLEVMA RTSPAYFVRF GAYQVLGLLQ DIEGVKSMRK DIRLSERDPK
     LKEMYEQFKD F
//