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Database: UniProt
Entry: D4ZGC6_SHEVD
LinkDB: D4ZGC6_SHEVD
Original site: D4ZGC6_SHEVD 
ID   D4ZGC6_SHEVD            Unreviewed;       874 AA.
AC   D4ZGC6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:BAJ00725.1};
GN   Name=pepN-1 {ECO:0000313|EMBL:BAJ00725.1};
GN   OrderedLocusNames=SVI_0754 {ECO:0000313|EMBL:BAJ00725.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ00725.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA   Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA   Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella violacea,
RT   a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; AP011177; BAJ00725.1; -; Genomic_DNA.
DR   RefSeq; WP_013050038.1; NC_014012.1.
DR   AlphaFoldDB; D4ZGC6; -.
DR   STRING; 637905.SVI_0754; -.
DR   KEGG; svo:SVI_0754; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_007335_1_1_6; -.
DR   OMA; CAYTNTG; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000002350; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
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   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:BAJ00725.1};
KW   Hydrolase {ECO:0000313|EMBL:BAJ00725.1};
KW   Protease {ECO:0000313|EMBL:BAJ00725.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..874
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003068719"
FT   DOMAIN          55..219
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          267..466
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          548..855
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   874 AA;  99024 MW;  EF226CE66972C3E3 CRC64;
     MNLLRACLLC LTSLLLISCN STSQSNVGDG NSLDSSSADK LALAKSRSAR ISEISYQLSL
     DLTQSEHFNG TTRITFKLSD TSTPLSLDLL RANIKSFVIN GHKIYPRYNG KAVILSPSTL
     VSGSNTVDIN YSQAYGTQGM GLVRFMDPKD GKVYLESNFC ADHASMMFPL FSQADLKASY
     SLNVTVPKTW LVISSVKEQK VIDSLESNLW QFPSSPKLSP HMFSLHAGPY RVWKDDTAKS
     KYPIRLFSRQ AIADDISPQI WFKDMDKGIR FMEEYLITPY PFSKFDMVLS PMMANDDAIA
     SAAVASISEN MTHHLAPLQQ RQKTIIKTTM TNLTAQWFGA LVTMNIWDES RLNMSLRSLI
     TKKTLAHLGY KSLDSKHFYD PIKAKAYVDD LLFTYHSDTS ILPSAGVHKS EAILQGLEQL
     IAEPDFRLGL QHYLTKFANK NVSAADFFAS LSLDNKHDLT QWQQDWFTTP GVNTIKAEFT
     CKNNRVSEFS LLQSSASKQH PRLREQKITL ALFTKGRNEL HRVRSISLVY KGERTRVRQL
     NGTRCPDLVY PNYLDSGYVK VSLDKRSLKT VKQHLNMVTE PQLRSMLWQS LWESVSDGEL
     ALNKYLDVVF INLPKEKEPV ILKQVLTNLN QSKTDLELIL KNHSSYIHMA LKGLEQMSLR
     KAMVNDENPN IQHLWFDAYI QFSHTPDSLT HLAKLLAGSS SIKGLKIDQE MRWKIVTQLN
     RYDYLGSRSL INKELNRDQS PRGRDAAIAA QVSRPEAGIK RYWLTHIQHD TNMPFSTLSI
     AMAHLYPREQ KILNSASSEQ RLESLAQLDA SKSDRFMKLY GQYLLPTRCD HRGLALLKST
     IDKQAGLSAT TQKALLQTHQ SELRCVAIKE HLLR
//
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