ID A0A081KDZ0_9GAMM Unreviewed; 881 AA.
AC A0A081KDZ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:KEI72366.1};
GN ORFNames=GV64_17980 {ECO:0000313|EMBL:KEI72366.1};
OS Endozoicomonas elysicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI72366.1, ECO:0000313|Proteomes:UP000027997};
RN [1] {ECO:0000313|EMBL:KEI72366.1, ECO:0000313|Proteomes:UP000027997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI72366.1,
RC ECO:0000313|Proteomes:UP000027997};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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:KEI72366.1}.
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DR EMBL; JOJP01000001; KEI72366.1; -; Genomic_DNA.
DR RefSeq; WP_026258424.1; NZ_JOJP01000001.1.
DR AlphaFoldDB; A0A081KDZ0; -.
DR STRING; 305900.GV64_17980; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000027997; 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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:0000313|EMBL:KEI72366.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000027997};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 113..196
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 239..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 454..554
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 558..881
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 881 AA; 100507 MW; 10A94EB83531906E CRC64;
MKDSQPKAIY LKDYQAPDYW IDQTNLTFDL YEDHTMVTSV LSIYRNLDNK SGKQGEDNLP
ELVLVGDDLE LISVEIDDKP FSDFKVEGGF LKILSLKESF TLKTVCRINP QENTSLEGLY
KSNGMFCTQC EAEGFRKITY YLDRPDVMSR FTTRITADKT AYPVLLSNGN DIERGELDDG
RHYVTWEDPF KKPSYLFALV AGDLQHVEDH FTTMSGREVT LRIFTEAHNI DQCDHAMISL
KKSMKWDEEV YGREYDLDIF MIVAVDHFNM GAMENKGLNI FNSACVLASP ETATDARFQR
VEAIVAHEYF HNWSGNRVTC RDWFQLSLKE GFTVFRDSEF SADMNSRGVK RIEDVNVLRT
AQFAEDAGPM AHPIRPESFI EISNFYTVTI YEKGAEVVRM IHGILGAEAF RKGSDLYFER
HDGQAVTCED FVKAMEDASG RDLTQFRRWY SQAGTPVLNI TDEYNEDKKQ YKLTIEQSCP
ATPGQKEKEP FHIPVRLGLL DAEGDELVLN ESGATDQVLD VKQEKEVFAF DNIEERPLPS
ILRSFSAPVR VKYDYSREDL LFLMEHDSDH FNRWDAGQRL ANSVIDEMVA AFEQGRELSV
DRSLIEAFGT VINDESLDLA VKAEMLSLPS EASLAEQAVE VYPQFIHQAR QQVKKAIAEA
HKDSLEALWQ SLNVHKPYRP EAEDIAERTL KNTCLSYLTS IEDKAMLALA EQQYHGASNM
TDRFAALVSV INAGNHDREL IDEVLADFLE LYHQDTNVMD QWLSVQAASP SLGTLEHILT
LMQHEVFDET SPNKLRSVLG GFAGNMKQFH RTDGLGYEFL TDQLLDLDKK NPQIASRLMT
PLTRWRKFEP GCRERMRKAL ERIKATPGLS SDVYEVVTKS L
//
