ID G8TWA6_SULAD Unreviewed; 1172 AA.
AC G8TWA6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=Sulac_0177 {ECO:0000313|EMBL:AEW03749.1};
OS Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=679936 {ECO:0000313|EMBL:AEW03749.1, ECO:0000313|Proteomes:UP000005439};
RN [1] {ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R.,
RA Gehrich-Schroeter G., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Sulfobacillus acidophilus DSM
RT 10332.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW03749.1, ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RX PubMed=23407703; DOI=10.4056/sigs.2736042;
RA Anderson I., Chertkov O., Chen A., Saunders E., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Han C., Tapia R.,
RA Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N.,
RA Pati A., Palaniappan K., Land M., Pan C., Rohde M., Pukall R., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Mavromatis K.;
RT "Complete genome sequence of the moderately thermophilic mineral-sulfide-
RT oxidizing firmicute Sulfobacillus acidophilus type strain (NAL(T)).";
RL Stand. Genomic Sci. 6:1-13(2012).
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; CP003179; AEW03749.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TWA6; -.
DR STRING; 679936.Sulac_0177; -.
DR KEGG; sap:Sulac_0177; -.
DR PATRIC; fig|679936.5.peg.182; -.
DR HOGENOM; CLU_005122_1_3_9; -.
DR Proteomes; UP000005439; 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 Gene3D; 2.40.10.170; -; 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; 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; 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:UP000005439}.
FT DOMAIN 633..794
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..969
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1172 AA; 131217 MW; 76C97149F2E8095F CRC64;
MGELASLLEL WSQYPPYQEL LNRFRNGGHT VQITGLSGSL PSFMVASLTE HIQRPALVVT
AGFQEARRLE AELEAYRPEA PLYLLPARPH IVGDVRAESY EWHERRLKAL DEAYHNPRAV
LVAPVEAVRQ RVVAMAQERI SLAPGQVIAP ETVAEQLVHL GYVRDPEVEQ EGHFAWRGAI
MDVFLPGGPA VRIEWFDDEV DSVRTFDPET QRTTQMLSRV SIGPARELIW SPEVLSRALA
RLGQESAEVI RNLEATGHFE EARRAEERYG RYWHDLSEGR SFPGVERFMA AFAAPKALVQ
VFSLKPLVIF HDLPRVLEAV RGQAVEAQLE RERRLERGDF LPVEAELDIP PESLLAELKG
WNTVHLSLMA HGSRRDEDVF SLTGRPAPRV HGQADLLKTE LTRLRKSRMK IGLVVRDEDA
RRLMMNHVLD SGLTPRPGLG VNGEIGVLLG TLSHGFVLPE LGLALLGETE LSGRDVKPET
RRRREARRTI RVGDLKPGDY VVHMTHGIGR FLGVRTLDIQ GQHKDYLHIQ YAGADTLYVP
VDQLGLVQKY VGVEGQEPRL SKMGGQEWTR TKEKVKASVR EMAEELLKLY AKREAEPGIA
YGPDTPWQAE FEAAFPYEET PDQLRAIDDI KRDMERARPM DRLLCGDVGY GKTEVALRAA
FKAIMGGKQV AFLVPTTLLA EQHYQTAKSR LAGYPVTVEV LSRFRTPKQQ KEILARVKKG
QVDLLVGTHR LLAKDVQFQD LGLLIVDEEH RFGVAHKERI KALKGNVDVL TLTATPIPRT
LHMALVGIRD MSVIETPPED RLPVETVVAE YDEDLVREAI RRELDRGGQV FYVQNRIRSM
DRTVEHLMKL FPGIRLAVVH GQMEENRIED VMARFIEQEY DILVTTNIIE SGLDIPNANT
LIVEDADKMG LAQLYQLRGR VGRSSRLAYA YFTFHPDKVL TPAAEKRLEA IREFTELGAG
YQIALRDLEI RGAGNLLGAE QHGFIATVGF DLYTQMLAQA VQELKGEPVE TPVDPTIEIA
VDAYLPDDYV PDPRQKIEMY KRLVSAKSLA EVEALAEEIE DRFGTAPASV TALVQLSRVR
VLARDVRLTQ VSHKGDRILL GGGPDSRVGP EAIQRLASRF PGRLIPGTQR APELGIKLPP
KASPDDALKT AEAVLTIMQE VSDHASAQTT HG
//
