ID V8CCH9_9HELI Unreviewed; 1062 AA.
AC V8CCH9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=HMPREF2086_00448 {ECO:0000313|EMBL:ETD25113.1};
OS Helicobacter macacae MIT 99-5501.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD25113.1, ECO:0000313|Proteomes:UP000018731};
RN [1] {ECO:0000313|EMBL:ETD25113.1, ECO:0000313|Proteomes:UP000018731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD25113.1,
RC ECO:0000313|Proteomes:UP000018731};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
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:ETD25113.1}.
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DR EMBL; AZJI01000001; ETD25113.1; -; Genomic_DNA.
DR RefSeq; WP_023927134.1; NZ_KI669454.1.
DR AlphaFoldDB; V8CCH9; -.
DR STRING; 1357400.HMPREF2086_00448; -.
DR PATRIC; fig|1357400.3.peg.603; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_2_7; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000018731; 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:UP000018731}.
FT DOMAIN 541..700
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 721..877
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1017..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 118979 MW; 12B43DC93E7E8119 CRC64;
MLQANLYRLL QSADSLGTSP RILLVANEKE ARQAYELACF VCAQSAHSPA NTSQNPPQNQ
KHTQDSSKAP FATPLLLPEA RFSKGEDLCS FYSEILQILA ILREFYERDD RLLIAPIYSL
LYAFPSQKHL QSFCLEVGKR YDLEELKEKI LCYGYEAVEV IEMEGEVSFR GDIIDIYPPL
SRPYRISFFD DECEDIRTFD TQTQLSDKDA KLDSLTLPPA LFALSEGECS ALLEAIENEL
DSSDSVFSKD ILSCGLWFLD KAGIDSCLLP QRFSTTITPN ALNELDEILS IRKDLDSFWH
SAKKSLPLLQ IANDYTDIDF YASSLLPIIT HNPHKKITLL CDSEAILSAL NIQELQKAHT
NIEILPINAN VNFATPRQIV LSLNPAQSYT KTRKKPKLQL DELNVGEYVV HSEYGIGIFR
GIVQDRILGA VRDFIAIDYQ GEDKLFLPVE NLHLIERYIA SSGSLPIVDR LGKGSFAKLK
QKARIKLFEL ADSIIKLAAQ RNLTKGLQID TNPPELEVFR HSSGFALTND QENAIKEIYE
DLSSGVVMDR LLSGDVGFGK TEVAMNAIYA VQKSGFQSAF IVPTTLLAAQ HFASLDSRLS
PLGVRIARLD RFCSAKDKRE ILKACKEGQI DVLIGTHSAF GVEFLRLGFV VIDEEHKFGV
KQKEGLKQMC KNAHILSMSA TPIPRTLNMA LSKIKGLSRL ETPPKERKDS RTFIKTKSPH
LLKEIISREV RRGGQVFYVH NNIAQIPALK SELAELFPHL SIAVLHSRIS ANDTEEIMRD
FMLKKYHILL CTAIVESGIH LPNANTIIID GADRFGLADL HQLRGRVGRG DKEGFCYFLI
ESVESITTEA KKRLLALERN SYLGSGASIA YHDLEIRGGG NLLGESQSGH IKNIGLSLYL
KMLEEAINIL SGSKIDDESD KGVELRLNVS AYLNPELIPS DRLRLEIYRR LSLCEEVGEV
AHIEREIEDR FGKLDEMSRA FLQLIVIKIL AQARGVAKIL HYEQNIQVEF RQSIKSPESS
ANYGNSRQDF GNNASDKSKI SLTSPSKDDE DVLEMILVFL CS
//