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Database: UniProt
Entry: I0SYV0_STRMT
LinkDB: I0SYV0_STRMT
Original site: I0SYV0_STRMT 
ID   I0SYV0_STRMT            Unreviewed;      1169 AA.
AC   I0SYV0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
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   ECO:0000313|EMBL:EID28553.1};
GN   ORFNames=HMPREF1048_0123 {ECO:0000313|EMBL:EID28553.1};
OS   Streptococcus mitis SK575.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1095736 {ECO:0000313|EMBL:EID28553.1, ECO:0000313|Proteomes:UP000005505};
RN   [1] {ECO:0000313|EMBL:EID28553.1, ECO:0000313|Proteomes:UP000005505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK575 {ECO:0000313|EMBL:EID28553.1,
RC   ECO:0000313|Proteomes:UP000005505};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EID28553.1}.
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DR   EMBL; AICU01000054; EID28553.1; -; Genomic_DNA.
DR   RefSeq; WP_000212600.1; NZ_AICU01000054.1.
DR   AlphaFoldDB; I0SYV0; -.
DR   PATRIC; fig|1095736.3.peg.761; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000005505; Unassembled WGS sequence.
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}.
FT   DOMAIN          627..788
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          809..963
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1169 AA;  134991 MW;  3A600AD88D1DBFBC CRC64;
     MATLLDLFSE NDQIQKWHQN LTDKKRQLML GLSTSTKALA IASSLKKEDK IVLLTSTYGE
     AEGLVSDLIS ILGEELVYPF LVDDSPMVEF LISSQEKIIS RVEALRFLTD SSKRGILVCN
     IAASRLILPS PNVFKDSIVK ISVGEEYDQH ALIHQLKEIG YRKVTQVQTQ GEFSLRGDIL
     DIFEISQLEP CRIEFFGDEV DGIRLFEVET QLSKENQTEL TIFPASDVIL REKDYQRGRS
     ALEKQVSKTL SPILKSYLEE ILSSFHQKQI HSDSRKFLSL CYDKTWTIFD YIEKDIPIFF
     DDYQKLMNQY EVFERELAQY FTEELQNSKA FSEMKYFADI EQIYKKQSPV TFFSNLQKGL
     GNLKFDQIYQ FNQYPMQEFF NQFSFLKEEI ERYKKMDYTI ILQSSNSMGS KTLEDVLEEY
     QIKLDSRDKS RICQESVNLI EGNLRHGFHF VDEKVLLITE HEIFQKKLKR RFRRQHVSNA
     ERLKDYNELE KGDYVVHHIH GIGQYLGIET IEIKGIHRDY VSVQYQNGDQ ISIPVEQIHL
     LSKYVSSDGK APKLNKLNDG HFKKAKQKVK NQVEDIADDL IKLYSERSQL KGFAFSADDE
     DQDAFDDAFP YVETDDQLRS IEEIKRDMQA SQPMDRLLVG DVGFGKTEVA MRAAFKAVND
     HKQVVVLVPT TVLAQQHYTN FKERFQNFAV NIDVLSRFRS KKEQTETLEK LKNGQVDILI
     GTHRVLSKDV VFADLGLMII DEEQRFGVKH KETLKELKKQ VDVLTLTATP IPRTLHMSML
     GIRDLSVIET PPTNRYPVQT YVLEKNDSVI RDAVLREMER GGQVYYLYNK VDTIDQKVSE
     LQELIPEASI GYVHGRMSEI QLENTLLDFI EGQYDILVTT TIIETGVDIP NANTLFIENA
     DHMGLSTLYQ LRGRVGRSNR IAYAYLMYRP EKSISEVSEK RLEAIKGFTE LGSGFKIAMR
     DLSIRGAGNL LGKSQSGFID SVGFELYSQL LEEAIAKRNG NANANTRTKG NAELILQIDA
     YLPDTYISDQ RHKIEIYKKI RQIDNRVNYE ELQEELMDRF GEYPDVVVYL LEIGLVKSYL
     DKVFVQRVER KDNKITIQFE KVTQRLFLAQ DYFKALSATN FKAGIAENKG LMELVFDVQN
     KKDYEILESL LIFGESLLEI KESKKENSI
//
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