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Database: UniProt
Entry: M3MAV5_HELPX
LinkDB: M3MAV5_HELPX
Original site: M3MAV5_HELPX 
ID   M3MAV5_HELPX            Unreviewed;      1001 AA.
AC   M3MAV5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=HMPREF1402_01284 {ECO:0000313|EMBL:EMG97537.1};
OS   Helicobacter pylori GAM121Aii.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1159030 {ECO:0000313|EMBL:EMG97537.1, ECO:0000313|Proteomes:UP000011875};
RN   [1] {ECO:0000313|EMBL:EMG97537.1, ECO:0000313|Proteomes:UP000011875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAM121Aii {ECO:0000313|EMBL:EMG97537.1,
RC   ECO:0000313|Proteomes:UP000011875};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA   Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2012) 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:EMG97537.1}.
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DR   EMBL; APDG01000062; EMG97537.1; -; Genomic_DNA.
DR   RefSeq; WP_001939480.1; NZ_KB636375.1.
DR   AlphaFoldDB; M3MAV5; -.
DR   PATRIC; fig|1159030.3.peg.1203; -.
DR   HOGENOM; CLU_005122_1_2_7; -.
DR   Proteomes; UP000011875; 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   CDD; cd18810; SF2_C_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; 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; 2.
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          499..658
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          671..835
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1001 AA;  113415 MW;  B6914FC7FA7F8FD0 CRC64;
     MIQSSLYKAL NKGFDYQILA CKDFKESRLA KEVISYFKPN TKAVLFPEFR AKRNDDLRSF
     FEEFLQLLGA LREFYQALEN KQETIIIAPI NALLHPLPKK ELLKSFKITL LEKYNLKDLK
     DKLFYYGYEI LDLVEVEGEA SFRGDIVDIY IPNSKAYRLS FFDAECESIK ELDPTTQMSL
     KEDLLEIEIP PTLFSLDEPS YKDLKTKVEQ SPLNSFSKDL TSFGLWFLGE KANDLLGVYQ
     SIISPKALEE IQELASLNEL DDERFKFLKV LENAQGYEDL EIHAHALEGF IALHSNHKIT
     LLAPNKTILD NAISALDAGN MECVIAPFVL NFKTPDRIFI SLNSFERKKK RQKSKLALNE
     LNPGEWVVHD DYGVGVFSQL IQHSVLGSKR DFLEIAYLGE DKLLLPVENL HLIARYVAQS
     DSVPVKDRLG KGSFLKLKAK VRTKLLEIAG KIIELAAERN LILGKKMDTH LAELEVFKSH
     AGFEYTSDQE KAIAEISRDL SSHRVMDRLL SGDVGFGKTE VAMHAIFCAF LNGFQSALVV
     PTTLLAHQHF ETLRARFENF GVKVARLDRY IKTSEKSKLL KAVELGLVDA LIGTHAILGA
     KFKNLGLMVV DEEHKFGVKQ KEALKELSKS VHFLSMSATP IPRTLNMALS QIKGISSLKT
     PPTDRKPSRT FLKEKNDELL KEIIHRELRR NGQIFYIHNH IASISKVKTK LEELIPKLKI
     AILHSQINAH ESEEIMLEFA KGNYQVLLCT SIVESGIHLP NANTIIIDNA QNFGLADLHQ
     LRGRVGRGKK EGFCYFLIED QKSLNEQALK RLLALEKNSY LGSGESIAYH DLEIRGGGNL
     LGQDQSGHIK NIGYALYTRM LEDAIYELSG GKKRLEKSVE IQLGVSAFLN PELIASDSLR
     LDLYRRLSLC EDVDEVGQIH EEIEDRFGKI DDLSAQFLQI ITLKILANQL GILKLSNFNQ
     NITLTYSDEK KESLKAPSKD DNDILETLLK HLHAQISLKR R
//
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