ID A0A085EKK3_9FLAO Unreviewed; 1122 AA.
AC A0A085EKK3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=FEM08_15290 {ECO:0000313|EMBL:KFC59748.1};
OS Flavobacterium gilvum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC59748.1, ECO:0000313|Proteomes:UP000028636};
RN [1] {ECO:0000313|EMBL:KFC59748.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1308 {ECO:0000313|EMBL:KFC59748.1};
RA Shin S.-K., Yi H.;
RT "Genome Sequence of Flavobacterium sp. EM1308.";
RL Submitted (MAY-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:KFC59748.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNCP01000038; KFC59748.1; -; Genomic_DNA.
DR RefSeq; WP_035636410.1; NZ_JNCP01000038.1.
DR AlphaFoldDB; A0A085EKK3; -.
DR STRING; 1492737.EM308_03550; -.
DR KEGG; fgl:EM308_03550; -.
DR PATRIC; fig|1492737.3.peg.1518; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000028636; 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; 3.
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 576..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 746..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 128538 MW; 5054A40C080DFC88 CRC64;
MSKATIYSVY DSSPKTTQIA ARLQENNQVK IQLEGLLGSA TSFVIQSVFK KAELPFLVVL
NNKEEAAYYL NDLEQMIGEQ DVLFYPGSFR RPYQIEETDN ANVLLRAEVL NRINSRKKPA
VIVTYPEALF EKVVTRQNLD KNTLKVTVGD KISIDFLNEV LFEYEFKRVD FITEPGEFSV
RGGIVDVFSF SNDNPYRIEF FGNEVESIRT FDVGSQLSLD KKKKITIIPN VENKVFQENR
ESFLDYIAES TVLFFQNTEN LLYELDKQFG KAEEAFEKLS KDIKHATPEQ LFLGQKEFVK
RALDFSIVEF NSKPVFKTTK KFEFHIQPQP SFNKQFDMLL NNLSDNHFNG YQNYLFCSNE
AQTKRFHDIF ESLDEANSEN IRKQYNTIVL PLYQGFIDQE NQICCYTDHQ IFERYHKFSI
KNGYSKKQNL TLKELTTLSV GDYVTHIDHG IGKFGGLQKI QVEGKTQEAI KLVYADNDIV
YVSIHSLHKI SKYNGKDGTP PKIYKLGSSA WKTLKQKTKA RVKHIAFNLI QLYAKRRLEK
GFQFAPDSYL QNELESSFIY EDTPDQIKST QEVKADMESE RPMDRLVCGD VGFGKTEVAI
RAAFKAVDNS KQVAILVPTT ILAYQHYRTF SERLKDMPVS IGYLNRFRTA KQKTETLKQL
AEGKLDIVIG THQLVNKNVV FKDLGLLIVD EEQKFGVNVK DKLKTIAANV DTLTLTATPI
PRTLQFSLMA ARDLSVITTP PPNRYPIETN VVGFNEELIR DAISYEIQRN GQVFFINNRI
ENIKEIAGMV QRLVPSARVG IGHGQMDGGK LEELMLAFMN GEFDVLVATT IIESGLDVPN
ANTIFINNAN NFGLSDLHQM RGRVGRSNKK AFCYFICPPY SHMTDDARKR IQALEQFSEL
GSGLNIAMKD LEIRGAGDLL GGEQSGFIND IGFDTYQKIM NEAIEELKEN EFKDLYPEEN
NIETKEYVKD LQIDTDFELL FSDEYINNVT ERLSLYNELA DVKNEEELIV FQNKLIDRFG
PMPPRALALM NSIRIKWIAT RVGIEKLVMK KGKMIGYFVS DQQSDFYHSK RFHKVIQFVQ
THSNICVMKE KQTPAGLRLL LTFDNVKNTR TALEFMQLLG GE
//
