(data stored in ACNUC7421 zone)

SWISSPROT: B8IT05_METNO

ID   B8IT05_METNO            Unreviewed;       685 AA.
AC   B8IT05;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   SubName: Full=Peptidase M3A and M3B thimet/oligopeptidase F {ECO:0000313|EMBL:ACL55067.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:ACL55067.1};
GN   OrderedLocusNames=Mnod_0016 {ECO:0000313|EMBL:ACL55067.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55067.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55067.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001349; ACL55067.1; -; Genomic_DNA.
DR   RefSeq; WP_012634306.1; NC_011894.1.
DR   STRING; 460265.Mnod_0016; -.
DR   MEROPS; M03.005; -.
DR   EnsemblBacteria; ACL55067; ACL55067; Mnod_0016.
DR   KEGG; mno:Mnod_0016; -.
DR   eggNOG; ENOG4105DGW; Bacteria.
DR   eggNOG; COG0339; LUCA.
DR   HOGENOM; HOG000245984; -.
DR   KO; K01284; -.
DR   OMA; KRSGAWC; -.
DR   OrthoDB; 1935578at2; -.
DR   BioCyc; MNOD460265:GCZK-16-MONOMER; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   InterPro; IPR034005; M3A_DCP.
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; B8IT05.
DR   SWISS-2DPAGE; B8IT05.
KW   Carboxypeptidase {ECO:0000313|EMBL:ACL55067.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435,
KW   ECO:0000313|EMBL:ACL55067.1};
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:UP000008207};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN      235    681       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   685 AA;  76205 MW;  ECF7952864B1447C CRC64;
     MAGTTATLPG NPFSEPVWTT PHGLPPFERI EPAHYEPAFT AALAEHEAEI AAIADSPEPP
     SFANTVAALE RSGQGLKRVS GVFFNITGSH TNPELQAVER IMAPRLARHR SALFLNGALW
     ARVKALDEAG LSEEERRVLD RYRTLFRRAG ADLDPAAKER VAAITARLAE LGTRFSQNLL
     ADESSFVLPL ETEEDLGGLP PFLRAAAARA AAERGLPGHV ITLARSLIEP FLVFSTRRDL
     RERAYTAWIR RGENGGETDN RAIIVETMRL RAERARLLGY ETFADFKLAD TMAGTPEAAM
     KLLREVWTPA RERAAAERDR LQAMVREEGG NFDLAPWDWR HYAEKLRRAE HDLDEGEIKP
     YLPLDGVIAA SFDTASRLFG LSFEELPAFP RYHPDVRAWA VKDRDGTTIG LFLGDYFARP
     SKRSGAWMSA FRSQERLIGP VTPIIVNVMN FAKGGEGEPS LLSFDDARTL FHEFGHALHG
     LLSDVTYPLL AGTAVAGDFV ELPSQLYEHW LEQPEVLRAH ARHYRTGEPM PEALLQRLLA
     ARTFNQGFAT VEYTASAIVD LDLHLSRAVE EGLDVNAFEA EALRRIGMPA EISMRHRSPH
     FAHIFTGEGY AAGYYSYLWS EVLDADAFDA FREAGDIFDP ETARRLRTYV YGAGNLRDAQ
     SAYTAFRGRL PSIEPLLRKR GLLAA
//

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