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Database: UniProt
Entry: A0A178M5A7_9PROT
LinkDB: A0A178M5A7_9PROT
Original site: A0A178M5A7_9PROT 
ID   A0A178M5A7_9PROT        Unreviewed;      1156 AA.
AC   A0A178M5A7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=A6A04_08650 {ECO:0000313|EMBL:OAN43942.1};
OS   Paramagnetospirillum marisnigri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN43942.1, ECO:0000313|Proteomes:UP000078428};
RN   [1] {ECO:0000313|EMBL:OAN43942.1, ECO:0000313|Proteomes:UP000078428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP-1 {ECO:0000313|EMBL:OAN43942.1,
RC   ECO:0000313|Proteomes:UP000078428};
RA   Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT   "Draft genome sequence of freshwater magnetotactic bacteria
RT   Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL   Submitted (APR-2016) 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:OAN43942.1}.
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DR   EMBL; LWQT01000120; OAN43942.1; -; Genomic_DNA.
DR   RefSeq; WP_068495738.1; NZ_LWQT01000120.1.
DR   AlphaFoldDB; A0A178M5A7; -.
DR   STRING; 1285242.A6A04_08650; -.
DR   Proteomes; UP000078428; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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}; 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:UP000078428}.
FT   DOMAIN          625..786
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          807..961
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1156 AA;  125206 MW;  1C2D7CDFBFFDA2FF CRC64;
     MKRLDDLISQ AGSFAVAGAP EGRDALLVAE LAASAGDILL VARDDGRMAR LAEALAFFAP
     DLPVLEFPAW DCVPYDRVSP NVDVVARRID TLARLADGGG QGPRLILTTV AALAQRVPPR
     EGLAKATLNA RPGASLSIER LVEFLHRSGY VRADTVMEPG EFAVRGGIVD LFPPGAAEPM
     RLDFFGDEIE AVRSFDPMSQ RTTGPVAGFS CRPVSEVGLD DASIARFRAA YRELFGVVQG
     ADPLYESISE GVKFTGMEHW LPLFHDGLDT LFAYCPEAAV VLDHQADEAL AARHALVLEY
     YDARVSMGGS GLAESGMVYH PVPPPKLYLE RDEWDRLLAV RPVLRLSPFD AMDGGAAFDA
     GGRLGRDFAD VRARPGVNLY DELRQHAEEQ AKTGRRVVVA AWTIGSRDRL AGLLKDHGLK
     GGETADSWTD VQALPKGKVA LAVLGLDHGF VTPDLALITE QDILGDRLAR PARKKKKGAQ
     FIAEASALSE GDLVVHVEHG IGRYDGLVAL QVAGAPHDCL RVLYDGGDKL FVPVENIEVL
     TRFGSDQSGV ALDKLGGTAW QARKAKLKKR IRDIADQLIG IAAQRQLRQG ETLTPAEGLY
     DEFCARFPWA ETDDQMRAIE DCVADLASGR PMDRLICGDV GFGKTEVALR AAFVAALQGL
     QVAVVVPTTL LARQHFRTFT ERFKGLPVRV EQLSRLVTAK TATAVKAGVA EGSVDIVVGT
     HALLAKGIGF KRLGLLIIDE EQHFGVAHKE RLKQLKSDVH VLTLTATPIP RTLQMALSGV
     KEMSVIATPP VDRLAVRTFV LPYDPVVLRE AILRERYRGG QVFYVCPRLA DIDRVAERLA
     KLVPEVKTAV AHGRLAPADL EEVMVAFGDK QYDVLLSTNI VESGLDMPSV NTLIIHRADM
     FGLGQLYQLR GRVGRGKTRG YAYFTLPNDK LLSKAAEKRL QVMQALDTLG AGFQLASHDL
     DIRGAGNLLG EEQSGHIREV GIELYQQLLE EAVAAAKGGT GAEAAEEWSP QIAIGSPVLI
     PDTYVADLSV RLGLYRRIAA LDTSEEIEAL AAELIDRFGK LPPEVENLLE VIAIKALCKQ
     AGIEKVDSGP KGAVVTFRGN VFANPVGLVQ FISRAGGSCK LRPDHKLVFL RNWEDPRDRV
     AGLRKVVGKM AELALA
//
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