ID D2Z3Z4_9BACT Unreviewed; 489 AA.
AC D2Z3Z4;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Excinuclease ABC, C subunit {ECO:0000313|EMBL:EFC92255.1};
GN ORFNames=Dpep_2233 {ECO:0000313|EMBL:EFC92255.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC92255.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC92255.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC92255.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFC92255.1}.
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DR EMBL; ABTR02000001; EFC92255.1; -; Genomic_DNA.
DR RefSeq; WP_005662162.1; NZ_ABTR02000001.1.
DR AlphaFoldDB; D2Z3Z4; -.
DR STRING; 469381.Dpep_2233; -.
DR PaxDb; 469381-Dpep_2233; -.
DR eggNOG; COG0322; Bacteria.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000006427; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd10434; GIY-YIG_UvrC_Cho; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR Gene3D; 3.30.420.340; UvrC, RNAse H endonuclease domain; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR001162; UvrC_RNase_H_dom.
DR InterPro; IPR038476; UvrC_RNase_H_dom_sf.
DR PANTHER; PTHR30562:SF1; UVRABC SYSTEM PROTEIN C; 1.
DR PANTHER; PTHR30562; UVRC/OXIDOREDUCTASE; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
DR PROSITE; PS50151; UVR; 1.
DR PROSITE; PS50165; UVRC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006427}.
FT DOMAIN 17..97
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 205..240
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 263..362
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 489 AA; 56092 MW; C8F7FB3F4B0A3A33 CRC64;
MTDRLERLKK LVRTFPNRPG VYLMHDSDGE IIYVGKAKSL KKRVSSYFRH ASGYASSRLR
KLVASIEDIS TIRTETEAEA LIVESRLIKK IMPFFNVDLK MNERYPYVYV TDDDFPRLEV
TLRKGEGLHI GPYVSAGELR RVLRLIERYF PLRTCRHDFS KVHLTRPCLR HSLGKCLAPC
VGLCSKGEYG DVLDDVVLLL RGQTLEVTDR LRKRMDRRAR EMRFEEAARL RDTLRALWRF
SRQKVSATLS ADLDEDTWQV LCDLQEIVGL PTVPWRIDGF DISHSSGHET YGVVVVFEQG
LPNPSLYRRF GIREVQGIDD FRSMKETVTR RYRKCLEGEA PLPQLILIDG GPEQLRFASE
ALSELGLSIP VMSLAKREEL VFTLDSEEPI ELERNDPALR LLQRVRDESH RYAITTHRGK
RQERLRRSAL EEIPGIGKRR AAALLARFGS VQQIARLGES ALMEVPGIGE SHARNILRHL
GGIDDEKQS
//
