(data stored in ACNUC7421 zone)

SWISSPROT: C3MF99_SINFN

ID   C3MF99_SINFN            Unreviewed;      1140 AA.
AC   C3MF99;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   SubName: Full=Putative restriction endonuclease type I with R subunit / type III with Res subunit {ECO:0000313|EMBL:ACP23936.1};
GN   OrderedLocusNames=NGR_c01330 {ECO:0000313|EMBL:ACP23936.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23936.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23936.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR   EMBL; CP001389; ACP23936.1; -; Genomic_DNA.
DR   RefSeq; WP_012706721.1; NC_012587.1.
DR   RefSeq; YP_002824689.1; NC_012587.1.
DR   STRING; 394.NGR_c01330; -.
DR   REBASE; 20749; Rsp234ORF1340P.
DR   EnsemblBacteria; ACP23936; ACP23936; NGR_c01330.
DR   GeneID; 7790712; -.
DR   KEGG; rhi:NGR_c01330; -.
DR   PATRIC; fig|394.7.peg.2927; -.
DR   eggNOG; ENOG4107SCJ; Bacteria.
DR   eggNOG; COG4096; LUCA.
DR   HOGENOM; HOG000295053; -.
DR   KO; K01153; -.
DR   OMA; HRSIYNL; -.
DR   OrthoDB; POG091H07NV; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006304; P:DNA modification; IEA:InterPro.
DR   InterPro; IPR025285; DUF4145.
DR   InterPro; IPR013670; EcoEI_R_C_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13643; DUF4145; 1.
DR   Pfam; PF08463; EcoEI_R_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
DR   PRODOM; C3MF99.
DR   SWISS-2DPAGE; C3MF99.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Endonuclease {ECO:0000313|EMBL:ACP23936.1};
KW   Hydrolase {ECO:0000313|EMBL:ACP23936.1};
KW   Nuclease {ECO:0000313|EMBL:ACP23936.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN      443    628       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      703    860       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   COILED      148    182       {ECO:0000256|SAM:Coils}.
FT   COILED      204    227       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1140 AA;  127450 MW;  32FDC6FCAC00F5B9 CRC64;
     MGGALSVNFD HLKSLSPELQ RLGTLAERFF ADDANTSLIK SRQFGEYMVK EIAALSGVYD
     PAARETTHDL LRRLATQQIL PREVADIFHA VRKSGNEATH NLAGSPTEAL AALKFCRALG
     VWYRRTYGRD PNFRPGPFVP PKASADIDQA TQAELATLRR QVREAEAQLA AAHSSADELA
     KARAAADELA RQAAADNAVW EQTAVEMEAN QAELSRKLAE LQKAAQAQPQ QLQMEFKQAG
     LQAASRLELD ERQTRRLIDA QLVDAGWEAD SDRLSYQLGA RPEEGRNLAI AEWPAAGGRA
     DYGLFIGLTC VGIIEAKRES VDVPSTLQQA ERYARTIALP PENSHPGGLW NHGLADPFRV
     PFVFTTNGRP FVRQWQTKSG IWFCDLRRDT NHPRPLTTWF SPKDLLDILA TDLDAAAQGL
     AEDSFGKGRM RPYQEDAIAA IENAVVAGQR DILVSMATGT GKTRTSIALM YRLLKHKRFR
     RILFLVDRKA LGKQTSDALE TTEIEGMLNF AQIYKVAGLE KKVPEDEDQV QVATVQSLIA
     RILNEPDPAK RPTPGTFDCI IVDEAHRGYT LDAELRESDV GFRNLDDYQS AYRQILDYFD
     AVKVALTATP ALHTREIFGH PVFHYGYRQA VVEGYLNDHL PPKRITTALS EAGIHFEGGE
     EVEIIDRTTG QIDLFELPDE VSLDYDVADF NKRVYSEAFN RMVCRAIATE IPPSKPGKTL
     IFAARDAHAD DLVRLLVEEL QEEYGNDAVP HGMVMKITGN VDKADDLILK FKNDPHPKYV
     VTVDLLTTGI DVPTICNLVF VRRVKSRILY DQMIGRATRL CPEIGKEHFR IFDAVDLYAE
     LQEMTDMRPV VVKPDISLGQ LVTDLDKAET EEDKSWVAGQ VIVRMRAMAN RMDAETRESF
     ERHTGETPEN AVQRLATLSG SELQDWLKSH PRVIELLERR PIRTGSGNDG VVISTHEDEL
     LRIEEIFGKN TTPEDYITGF ERFIRENMNQ VPALIAVTQR PRDLTRKELS ELAGLLDEKN
     YSEAMLRAAY GKVRNADIAA HIIGFVRQAA IGDPLIPYAT RVENAIGKIE ASRPWTQKQK
     EWLRRIGRAL KDKPVADPTL LDQGVFADKG GFKRISQEFD GELDDVLHAF NEAIWAPPAA
//

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