ID Q21JS3_SACD2 Unreviewed; 1153 AA.
AC Q21JS3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 118.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN OrderedLocusNames=Sde_1796 {ECO:0000313|EMBL:ABD81056.1};
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD81056.1, ECO:0000313|Proteomes:UP000001947};
RN [1] {ECO:0000313|EMBL:ABD81056.1, ECO:0000313|Proteomes:UP000001947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024
RC {ECO:0000313|Proteomes:UP000001947};
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR EMBL; CP000282; ABD81056.1; -; Genomic_DNA.
DR RefSeq; WP_011468276.1; NC_007912.1.
DR AlphaFoldDB; Q21JS3; -.
DR STRING; 203122.Sde_1796; -.
DR KEGG; sde:Sde_1796; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_6; -.
DR OMA; WAPPCRE; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000001947; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR CDD; cd18810; SF2_C_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11140; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR048635; MFD_D3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21132; MFD_D3; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF143517; TRCF domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000001947}.
FT DOMAIN 622..783
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 804..960
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1153 AA; 130334 MW; D3030B6B1A8A01CC CRC64;
MTSNMPLPLP SKLGDKKTWG GVSGLARVFA CAEAAAQHNG TTVIIVQSMT EADRFARDLM
LLTKGKKNTP EVLQFADWET LPYDNFSPHQ DIISDRMRCL YQLSNQAQAI VVVAASTLMQ
RLAPANYIIA NSLVVEKNET INRDNLLTSL INAGYQRVDT VFNHGEFAIR GALLDIFPMG
SSAAYRIELF DDEVDSIRTF DPETQRTVDQ VSKIELLPGK ECQLDAEGIS RFKLNWYENF
NVDHRECPVF QDVSSGISPA GIEYYLPLFF EQTASLFDYL HENTLVMVTK GFETAVEDFW
RDASSRFESH NIDMRRPLLP PAKVFHSVSE IYSQLKRFQR VVLEPTQVEE RSGSANIKTL
STPNLNIDAK AQNPLYKLEE FIYSYDGRIL FCAESNGRRE TLKEHFKKID LQPEDVASTD
AFLQGKSSIA ICVADFQEGL HLKTPNICII AESQLFGQRV QQYRRRKESN TDFNENIVKN
LTELKIGAPV VHIEHGVGRY LGLQTIEFDG QKDEFLVLEY ANEAKLYVPV ANLHFISRYS
GAEDSSAPLN RLGSDQWQKA KRKAAEKLRD VAAELLEIYA KRQAREGFQY TYPKDAYEIF
AESFPFEETV DQQQAIDAVR QDMISAQPMD RLVCGDVGFG KTEVAMRAAF IAVQNSKQVA
VLVPTTLLAQ QHYENFKDRF ADWPVNVEVI SRFKSSKDIS EIQKKLEAGK VDILIGTHKL
IQGELIFPNL GLLIIDEEHR FGVRQKEALK ALRTEVDILT LTATPIPRTL NMAMSGIRDL
SIIATPPAKR LSVKTFVRQS DNAVIKEAIL REIMRGGQLY YLHNEVSTIE KTAADLQELV
PEARIRVAHG QMRERELEAA MSDFYHKRHN ILVCTTIIET GIDIPSANTI IIDRADKFGL
AQLHQLRGRV GRSHHQAYAY LLTPHKKAMT ADAVKRLEAI AEAQDLGAGF TLASHDLEIR
GAGELLGDEQ SGQMQAIGFS LYMEMLDKAV EALKSGKELD FESNFNNNVE FNLRIPALIP
DDYLPDVHTR VILYKRMASV KNENELNDLQ VEMIDRFGLL PDPIKNLVRQ TRLRLTAEQL
GVCKVEANNT GGRIEFTTKP NIDPLTIVKM VQTTPQHYRM EGASHLKFFF DMESADERLL
TIHNIFETLM KSS
//