ID A0A1C4RP92_9ACTN Unreviewed; 841 AA.
AC A0A1C4RP92;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=GA0115240_154753 {ECO:0000313|EMBL:SCE36770.1};
OS Streptomyces sp. DvalAA-14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCE36770.1, ECO:0000313|Proteomes:UP000199020};
RN [1] {ECO:0000313|EMBL:SCE36770.1, ECO:0000313|Proteomes:UP000199020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCE36770.1,
RC ECO:0000313|Proteomes:UP000199020};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMCH01000493; SCE36770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4RP92; -.
DR Proteomes; UP000199020; 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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_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:SCE36770.1};
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:UP000199020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 121..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 526..835
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 701..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 91048 MW; 6585E32FE5B1BF58 CRC64;
MSDPGELRQH AGMPALLRTE AVIRARLLDV RSCFVALDVS RGDRIFRSTT VIRFACAEPG
AESFVEIEPA VLHRVELNGR ALDPAVVGAN RLRLPDLAAE NELLVDADMA YSHTAEGLHH
FTDPADGAGY VYASCGPDLA PKIFACFDQP DMKAPFTFTV TAPDGWTVIG NGSADQRADG
RWEIAPVGPI STYLTTLVAG PLHAVRAEHD GIPLGLYARR SLAAELDREA PDLFEVTRAS
LDRLHELFEE RYPFGGYDQA FMPEFNWGAM ENPGCVIFRD EMLFRSAPTD AQRTLRAVVV
CHEMAHMWFG DLVTLGWWDD VWLNESFAEV LGYRIAAEAT RYTDSWTLFA ARRKSWGYDA
DQRPTTHPVA ATGATSAAEA LSGFDGISYA KGASALRQLA HRLGDERFFA GLNAYFAAHR
WGNADLGDFL AALSTADSSP DVSDWADLWL RTSGVDTLRI EVEAADGAVT SAVLVNNGSR
PHRVRIGVYV WDGAAITARQ RLDASVDPGG RTPLPELAGA PRPALLLPND GDLTWARIRL
DEQSAATVAA SLSAVRDELA RAVLWEHARH LTRSAELPAD RYLRMVADHL PVETSDSVLE
AVLTFATDHV VARYLDPADR PAALVLLGDT ARAVLTRPDA GRGLRIAALH ATIATATGDD
RLAELTGWLA GRDLPGGLPF DADLRWAALA RLAATGAAGE EQIAAEQSSD ASDTGEQGAA
RARAALPDDA AKDRAWRRLF TPGALSNRLL AATAEGFWRS GAPQRQQDYV RRYFEQIPAV
GDRGGAVVKA LGQGLFPTGA ATADTLRAAE ACLARPDVTP LLRRHLADGL DDLRRAYAHR
L
//
