ID D7B3Q1_NOCDD Unreviewed; 848 AA.
AC D7B3Q1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
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 OrderedLocusNames=Ndas_3413 {ECO:0000313|EMBL:ADH68818.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68818.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH68818.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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; CP002040; ADH68818.1; -; Genomic_DNA.
DR RefSeq; WP_013154425.1; NC_014210.1.
DR AlphaFoldDB; D7B3Q1; -.
DR STRING; 446468.Ndas_3413; -.
DR MEROPS; M01.009; -.
DR KEGG; nda:Ndas_3413; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OMA; CAYTNTG; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000002219; Chromosome 1.
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:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:ADH68818.1}; 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:UP000002219};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 228..441
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 523..832
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 848 AA; 94045 MW; CE970DF3C1F6AF25 CRC64;
MAGNLTRDEA RERARILSVD SYAVELDLTT GAETFRSTTV IRFSSSEPGA RTFVELAAPA
IRTATLNGAE LDAAELFDGE RLVLPEVAAD NELTVVADAV YMRTGEGLHR FVDPVDDSVY
LYTQFETADA HRMFACFDQP DLKATFELTV FAPPSWEVVS NSAPDVEREA AGEERVRWHF
PATPVMSTYI TALIAGPYHV VRDEHDGIPL GLYCRASLAE HLDSDALFEV TKQGFDFFHG
LFDLRYPFGK YDQLFVPEFN AGAMENAGAV TFLEDYVFRS RVTDARYERR AETILHEMAH
MWFGDLVTMR WWDDLWLNES FATYASVYCQ ANATKWTDAW TTFANVEKSW ALRQDQLPST
HPVAADMVDI QAVEVNFDGI TYAKGASVLK QLAAYVGVDA FFAGVRAYFK ENAFGNTELR
DLLKHLEAAS GRDLSGWSRD WLETTGVNTM RPEFEVDAEG RFTSFTVLQE APADHPTLRS
HRLAIGLYDR TDEGVVRRER VELDVRGERT EVPELVGRVR PDLVLINDDD LTFTKVRLDE
RSLRTVVEGV GEIRESLPRA LAFGAAWDMT RDGEMAARDY VSLVISGISG VDDVMVAQTL
LRQANSALHM YADPAWRPFG FEQLSERLRE LLTAAEPGGD LQLAYANALA ASAASDAHLS
LLQGLLDGAI TVDGLVVDTD LRWTLLRRLV ATGKAGEAEI AAELERDATA AGQRNAAGAR
AAIPTAEAKA AAWERIVGEE LANAEFRAVL LGFTEPGQAE LYRPYVERYF AQLGPAWEKW
TGEFAQTFAE VVYPSGLVEE ATLERTDAYI AESDPAPALR RLLVEGRAGV ERALRARATD
IAAGERQE
//