(data stored in ACNUC7421 zone)

SWISSPROT: A0KFW9_AERHH

ID   A0KFW9_AERHH            Unreviewed;       615 AA.
AC   A0KFW9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ABK37892.1};
GN   OrderedLocusNames=AHA_0612 {ECO:0000313|EMBL:ABK37892.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37892.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37892.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP000462; ABK37892.1; -; Genomic_DNA.
DR   RefSeq; WP_011704579.1; NC_008570.1.
DR   RefSeq; YP_855151.1; NC_008570.1.
DR   STRING; 380703.AHA_0612; -.
DR   EnsemblBacteria; ABK37892; ABK37892; AHA_0612.
DR   GeneID; 4490159; -.
DR   KEGG; aha:AHA_0612; -.
DR   PATRIC; fig|380703.7.peg.610; -.
DR   eggNOG; ENOG4108K0S; Bacteria.
DR   eggNOG; COG1164; LUCA.
DR   HOGENOM; HOG000271641; -.
DR   OMA; FDYKVNK; -.
DR   BioCyc; AHYD380703:G1G7B-613-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   Gene3D; 1.10.1370.10; -; 2.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFW9.
DR   SWISS-2DPAGE; A0KFW9.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN      138    542       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
FT   COILED      209    229       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   615 AA;  68397 MW;  4A569374A1653BBF CRC64;
     MSSIARNYLN QLNADYLQVH RRKEDLFWST YMGTSDDQAG FTAAEQAYKA FCADPARLPV
     LRQMQAQAEE TELKRGLGGW IAFFECNVIE DPQAAALMDE LVAAEAALFA RRRELKLTLL
     DEQGRQVAGS LPAASTALAA SSDEAVRQSA LAMFHTLEQW VVDNGYLAIV ALRNRFARAM
     GYRDYFDYKV HKNEQMSPAQ LFAILDDFIA GTEQRLHQSL AELKAAKGEA ALLPHNLRYS
     VSGDVTRQLD PYVPFSRALQ DWVESFRRLG IQYRGATLTL DLLTREGKYE NGFCHGPVPS
     FWQEGEWVPA VVNFTSLANP AQVGSGWSGL NTLFHEGGHA AHFANVTGNA PCFSQEFPPT
     SMAYAETQSM FCDSLLDDAD WLKRYARNAA GEPIPDALIK AMIEARQPFR AFNERQIALV
     AYFERDLYAM DEAERTPAAV LVLARRWERK ILGGESPRPL LAIPHLLNQE SACAYHGYLL
     ALMAVEQTRA YFLKRDGYLT DNPRIGPDLA AHYWGPGNGM THDETLQSLT GKGFSAGPLA
     RACNQSVAEA WQQAEACMAA ARQRPPVGEG EPLNARIRVV HGDQLIADNS GSEAAMLADF
     ECWIRDHYQE TVTSH
//

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