ID A0A372IY71_9ACTN Unreviewed; 849 AA.
AC A0A372IY71;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=pepN {ECO:0000313|EMBL:RFU19884.1};
GN ORFNames=D0Z06_19010 {ECO:0000313|EMBL:RFU19884.1};
OS Geodermatophilus sp. LHW52908.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2303986 {ECO:0000313|EMBL:RFU19884.1, ECO:0000313|Proteomes:UP000262362};
RN [1] {ECO:0000313|EMBL:RFU19884.1, ECO:0000313|Proteomes:UP000262362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52908 {ECO:0000313|EMBL:RFU19884.1,
RC ECO:0000313|Proteomes:UP000262362};
RA Li L., Lin H.W.;
RT "Geodermatophilus marinus sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-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:RFU19884.1}.
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DR EMBL; QVQH01000021; RFU19884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372IY71; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000262362; 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:RFU19884.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RFU19884.1};
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:UP000262362};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 103..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..446
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 528..837
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 706..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 93641 MW; 5223583C8986ABA1 CRC64;
MAVPNLTREN AAARARLLAI GGYDLRFDLT DGAGRPGEGT FRSTTTVRFT CREPGAGTSI
DLVAERVRSA TLNGVPLDVA TWTEEDGLPL PGLAAENTLV VDADCRYSNS GEGLHRFVDP
EDAQVYLYTH FEPADAKRVF ACFDQPDLKA TFAVHVTAPF DWQVVSNSGE RTVEAGPGGS
QLVHFAATKR LSTYLLALVA GPYARVTDSH EGIPLGLYCR ASLAQHLDPE ELFRVTKQGF
DFYQRVFDYP YPFDKYDQLF VPEFNAGAME NAGAVTFLED YVFRSRATRA RYERRAETVL
HELAHMWFGD LVTMRWWDDL WLNESFATYI SVLCQAEATE YATAWTTFAN SEKAWAYAQD
QLPSTHPVAA DMVDVAAVEV NFDGITYAKG ASVLKQLVAY VGREEFLAGI RRYFRAHEYG
NTTLADLLDP LSEATGRDLS EWSRQWLETS QVNTLRPVLE LSDDGRYRSF AIEQTAVPEH
PVLRRHRLAV GLYSAGPEGL TRTHRVELDV DGERTEVPEL AGHPAADLVL VNDEDLTYAK
LRLDERSLAT LQRSIADIPD SLARALCWSA AWDMTRDAEL PARDWVGLVL AGVDAETEIS
VVQSLLARVQ SALTSYADPQ WAESGWRALA DKALAALQTA EPGSDVQLQW SRTLAAAART
EEHAAVLRGL LDGSRVIEGC AVDADARWAF LNGLVAIGAA GDAEIDAEEE RDPTATGQRR
AATARALRPT AAAKEETWSR TFTDDTLPNA VHEAMVGGFW HPAQRELTAG YVDRYFAEIG
PFWAHRPGEI AKNAVQYLFP PVVEQRTLDA ADAWLADGAH PAPLRRLVTE GRDGIARALR
ARERDTAAG
//
