ID A0A1T5B4P7_9FLAO Unreviewed; 1122 AA.
AC A0A1T5B4P7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN05660866_01396 {ECO:0000313|EMBL:SKB42039.1};
OS Maribacter arcticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=561365 {ECO:0000313|EMBL:SKB42039.1, ECO:0000313|Proteomes:UP000190339};
RN [1] {ECO:0000313|EMBL:SKB42039.1, ECO:0000313|Proteomes:UP000190339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23546 {ECO:0000313|EMBL:SKB42039.1,
RC ECO:0000313|Proteomes:UP000190339};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUYL01000003; SKB42039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5B4P7; -.
DR STRING; 561365.SAMN05660866_01396; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000190339; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SKB42039.1};
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 571..732
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 741..907
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 128949 MW; 22CCC6819E5EB19F CRC64;
MSHSSIQQQY GQSPQIGKLL NTIADSENSG TKNIQLKGLI GSSLSFVLAN IFKTVDRPFL
AIFNDKEEAA YYLNDLERLI GEDDVLFYPG SYRRPYQIEE TDNANVLLRA EVLNRINSRK
KPAIIVTYPD ALFEKVVTRK ELDKNTLKMK LGDTLSLDFL NEILFEYKFK RVDFVTEPGE
FSVRGGIVDV YSFSHDEPYR IEFFGDEIDS IRTFDVETQL SKEKVKSITI VPNMANKFLT
EKRQSFLTYV ASKTLVFAKN TDFLYDRLDD FFEKAKEAFT KLSKDIKHAE PEELFMGGTE
FRKHLSDFTL LTQDSKRNSE SLVEFHTKPQ PSFNKKFDLL IENLNGYREQ GYTNYIFCAS
EQQAKRFHDI FEEVNEQVHY QIIVFPLFQG FVDDDQKLVC YTDHQIFERY HKFHVKNGYA
KKQAITLKEL NKLEIGDYVT HIDHGIGKFG GLQKIDVEGK KQEAIKLMYG ERDILYVSIH
SLHKISKFNG KDGTPPKIYK LGSGAWKKIK DKTKSRVKKI AFNLIKVYAK RRLEKGFQYN
PDSYLQNELE ASFIYEDTPD QSTATEDVKR DMESERPMDR LICGDVGFGK TEIAIRAAFK
AVDNGKQVAI LVPTTILAFQ HHRTFTERLK DMPVTVDYLN RFRTAKEKKD TIERLAAGKV
DIIIGTHQLV NKNVQFKDLG LLIVDEEQKF GVAVKDKLKS IKENVDVLTL TATPIPRTLQ
FSLMAARDLS TITTAPPNRY PIESQVVRFN EEIIRDAVSY EIERGGQVFF IHNRIENIKE
VAGLIQRLVP DAKVAVGHGQ MEGKKLEALM LAFMNSEFDV LVSTTIVESG LDVTNANTIF
INNANNFGLS DLHQMRGRVG RGNKKAFCYF ITPPYEVMTN DARKRIEALE QFTELGSGFN
IAMKDLEIRG AGDLLGGEQS GFINEIGFET YQKILAEAID ELKENEFKDL YDEVEGPHEK
IFVKETQIDS DFELLFPDDY INNITERLTL YTDLNQVKDE QALQKFEEQL VDRFGELPDQ
AADLLNSVRI KWISNSIGLE KIVMKQGKMI GYFISDQQSA FYQTPTFTRV LQYVQSHAQQ
CKIKEKQTRN GLRLLLVFEN IRSVDRAYLA LKPFEIKEKQ FV
//
