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Database: UniProt
Entry: D7B3Q1_NOCDD
LinkDB: D7B3Q1_NOCDD
Original site: D7B3Q1_NOCDD 
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
//
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