ID A0A3D8IZ56_9HELI Unreviewed; 968 AA.
AC A0A3D8IZ56;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:RDU70185.1};
GN ORFNames=CQA62_01245 {ECO:0000313|EMBL:RDU70185.1};
OS Helicobacter cholecystus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=45498 {ECO:0000313|EMBL:RDU70185.1, ECO:0000313|Proteomes:UP000257067};
RN [1] {ECO:0000313|EMBL:RDU70185.1, ECO:0000313|Proteomes:UP000257067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700242 {ECO:0000313|EMBL:RDU70185.1,
RC ECO:0000313|Proteomes:UP000257067};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-2018) 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:RDU70185.1}.
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DR EMBL; NXLU01000001; RDU70185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8IZ56; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000257067; 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 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; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR30580; PRIMOSOMAL PROTEIN N; 1.
DR PANTHER; PTHR30580:SF0; PRIMOSOMAL PROTEIN N; 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}; Reference proteome {ECO:0000313|Proteomes:UP000257067}.
FT DOMAIN 472..629
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 650..802
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 968 AA; 109519 MW; F651576B911F6EA6 CRC64;
MAFETLDYLS PQSQIKPFLL PELRIVFGDD LRSYFQELSA LSHTLRNYYA FEGKKILIAP
ILSVMYALPS AQHLQSFWIQ KEQNYSIQEL KEKLSLYGYE FVDFVETEGE VSIRGDIMDI
FIPHHPNPYR ISFFDVFVEE IKEFELESQL CLEGEVQSIE ITPPFFSLSE DEEKTIQETI
QKQDFQSLSQ DVQGLGFWFL PHKILLPQVL STALTQEAKS EAIEFFSFQE QSDLGENDLE
KCRVLEPIEG YSDILFDIKN LELLLAHQDK QITLLCNNSS VFENLKFHYN LEGVTLKTSP
HIINILTPTE LILSLNTFSS KTKTKKPKIL LDELKIGEYI VHQDYGIGIF RGIVQTEIIG
SVRDFIQIDY QGEDKLLLPV ENLHLIDRYI ANSGNVPILD RLGKGAFIKL RDKVKTKLFE
IAQGIIALAA KRDLLEGCKI DITNPEIKVF QNACNFILTQ DQERSICEIF NDLCSGKVMD
RLLSGDVGFG KTEVAMNAIF AVCKSGYQCA LIAPTTLLSS QHFASLQARF EGFNITLAKL
DSTIKNKSAV LKNLAEGNIN VIVGTQALLN ATFKNLGLVV VDEEHKFGVK QKEKIKELSS
NVHLLSMSAT PIPRTLNMAL SQIKGMSSLL TPPNEREGVR TFVKNYSDSL LKEAISRELR
RGGQVFFIHN HIASIQKRKE KLLELMPSLK IALLHSQIQN SEEIMEDFFN KKYNLLLCTS
IVESGIHLSN ANTMIVEGAD RFGIADLHQL RGRVGRGNKE GFCYFLIEDR ESLGEEAKKR
LLALEQNSYL GSGASLAYHD LEIRGGGNLL GEAQSGHIKN IGYGLYLRML EECINALSGK
EKLQAKSVEL KLNVSAYLNP ELIASDRLRL ELYRRLSLCK SVEEVFKIQA EIEDRFGKPD
IYTKQFLDLI IIKILGSLCN LKMISNYGQN ITFLYNDGTK ETLKSASKDD DDVIAMILQT
LRKKQKAL
//