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Database: UniProt
Entry: V8CCH9_9HELI
LinkDB: V8CCH9_9HELI
Original site: V8CCH9_9HELI 
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
//
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