ID   A0A1M6RAC1_9BACT        Unreviewed;       863 AA.
AC   A0A1M6RAC1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=SAMN02746009_00643 {ECO:0000313|EMBL:SHK29366.1};
OS   Hymenobacter psychrotolerans DSM 18569.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1121959 {ECO:0000313|EMBL:SHK29366.1, ECO:0000313|Proteomes:UP000183947};
RN   [1] {ECO:0000313|Proteomes:UP000183947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18569 {ECO:0000313|Proteomes:UP000183947};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FRAS01000002; SHK29366.1; -; Genomic_DNA.
DR   RefSeq; WP_073281266.1; NZ_FRAS01000002.1.
DR   AlphaFoldDB; A0A1M6RAC1; -.
DR   STRING; 1121959.SAMN02746009_00643; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000183947; 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; PF13646; HEAT_2; 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   Aminopeptidase {ECO:0000313|EMBL:SHK29366.1};
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          79..266
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          304..512
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          24..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97624 MW;  80659059D7D6A81A CRC64;
     MKYPIFGILA LVLTCQFEAP AQAVKSGKPT GNKAATHRKT EPPAAPAPAP ATVVVPSWLP
     PTSPVQPAAT ILHDLLDTKL DVRFDWNKQW VLGTAVLTVR PHFYPQNQLV LDAKGFEVKS
     VKLLSGSKEK NLSYTYDKKK LTISLDRAYT RTEPCQVRIQ YVAKPNELEA GGSAAITQDK
     GLYFVNPLGT DKTKPRQIWT QGETEGSSCW FPTIDRPNQR MTQEISLTVE ASLKTLSNGL
     LTASRKNNDG TRTDTWKQTL PHAPYLTMLA VGNFAVVSDT WRGKAVDYYV DPQYSATAKA
     VFGNTPEMLD FFSQKLGVEF PWEKYSQIAV HDFVSGAMEN TTAVTFEQSL VQFTARELPD
     IGYDPEATVA HELFHHWFGD YVTSESWANL PLNESFADYS ELLWAEHKYG ADAAALVQQE
     KMGRYLDEAQ SKREPLIRYQ YAHHEDMFDR HSYDKGGRVL HMLRKYVGDD AFFTSLNRYL
     TQNKFSASEI AKLRIAFEET TGEDLMWFFD QWFMKRGHPE LKVTHSFVNG QVSLRVQQLQ
     DSTFTPIYRL PVGVTVWANN QPTEHRVLIT KADQTFRLPS SQRPALVKFD SESQLLAEID
     EERSQEELLY QFSHARNYLQ KYEAISRLRT KSADLAVSGM LRAALNDNFW AVRQAAVEAL
     RRYKGPEGEA VRKDLQRVAA SDKKSQVRAT ALATLSAFNN ENYSGLYLAA LNDSSYKVVS
     AAIRALAKTP TADSQDRITA FQETKNQEVL SAISTYFSLN GSSTEQYQWF LRRLPEVSEA
     DLYRTYLPNF ATFMLRIPPI EREKGVQKLE SLARTAHNSI VRLGAYRGLS ILATGMPTLK
     TVMQDIRSKE KDEQVKAYYA LMQ
//