ID A0A0A6XXI3_9FLAO Unreviewed; 1104 AA.
AC A0A0A6XXI3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ORFNames=HMPREF9074_09452 {ECO:0000313|EMBL:KHE67894.1};
OS Capnocytophaga sp. oral taxon 329 str. F0087.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE67894.1, ECO:0000313|Proteomes:UP000030579};
RN [1] {ECO:0000313|EMBL:KHE67894.1, ECO:0000313|Proteomes:UP000030579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0087 {ECO:0000313|EMBL:KHE67894.1,
RC ECO:0000313|Proteomes:UP000030579};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2014) 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:KHE67894.1}.
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DR EMBL; AFHP02000235; KHE67894.1; -; Genomic_DNA.
DR RefSeq; WP_009389422.1; NZ_KN390076.1.
DR AlphaFoldDB; A0A0A6XXI3; -.
DR STRING; 706436.HMPREF9074_09452; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_10; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000030579; 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; 3.40.50.300; 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 561..722
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 731..897
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1104 AA; 125617 MW; 66ACD2486C709C40 CRC64;
MKELLQSLAQ SSLYKSLLAK VQAQNSTTVG GLAGASLSAV VANLYTHTHR PLLVLLPDKE
ESAYVLNDLE TLVGEQRVLF FPDSYRRPYQ IEDTDNANVL LRAEVLHQLS HSTKPLIVVS
YPEALFEKVI TRKQLEQNTL KITKGDSLTL EFLNEVLFSY QFNRTDFVTE PGEFSVRGGI
VDIFSFSNNE PYRIEFFGNE VESIRTFDVE SQLSTAQLSQ IIIIPNVENK ESDEVRQSFL
EYISPQTLFI AKDIASLGQK IDKLFAKATD IYQKLANEVK RTAPEELYCQ TEDLLAQANR
LQSIHIGISQ PELTFLTTPQ PSFNRQFELL IAYLNEKHAE GYQNYILCGT EQQAKRFHDI
FEEMEQKVAY QTVQLSLHAG FVDNELKINV FTDHQIFERY YKFQLKNGYA KKQAITLKEL
MQLEVGDYVT HIDHGIGKFA GLQKIEVEGK QQEAIKLIYG DRDVLFVSIH ALHKITKYNG
KDGKPPKIYK LGSGAWKALK QKTKARVKEI AFNLIQLYAK RKEAQGYAFA HDSYMQNELE
ASFLYEDTPD QSKATAEVKA DMESAKPMDR LVCGDVGFGK TEVAIRAAFK AVDNGKQVAV
LVPTTVLAFQ HYQTFSQRMK DFPVRIDYLN RFRTAKEKKI ILEELAKGQL DIVIGTHQIV
GEKVQYKDLG LLIVDEEQKF GVGVKDKLKT LKENLDVLTL TATPIPRTLQ FSLMAARDLS
VINTPPPNRY PIDSQVIPFS EEVIRDGIRY EIQRGGQVFF MHNRVENIQE VAGMIQRLLP
DARIAIGHGQ MDGKKLEETM LAFMEGAYDV LVATTIIESG LDVPNANTIF INNAHNFGLS
DLHQMRGRVG RSNKKAFCYF ITPPLIAMSD DARKRIEAIA QFSDLGSGLN IAMKDLEIRG
AGDLLGGEQS GFINEIGFDT YQKILQEAIT ELKENEFSEL YRTAEEDKTY LTDTQIDTDF
ELLFPDTYVN RVAERLNLYN ELSNLTNEEA LQVYQRNLID RFGKLPPQAI DLLNSVRVKW
LATRMGIEKL VMKNGKMTGY FIADQNSPFY QSARFQKLLL FVQRYPNQCR MQEKETRNGL
RLLILFDGIN TVYQALKVLQ QIEA
//
