ID A0A1Y2K635_9PROT Unreviewed; 1189 AA.
AC A0A1Y2K635;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=MAIT1_03131 {ECO:0000313|EMBL:OSM05003.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM05003.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM05003.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM05003.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
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:OSM05003.1}.
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DR EMBL; LVJN01000018; OSM05003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2K635; -.
DR STRING; 1434232.MAIT1_03131; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000194003; 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:UP000194003}.
FT DOMAIN 640..801
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 822..976
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1189 AA; 131917 MW; 402FA50BD41A507B CRC64;
MTDAPLSPVL APLRQALDRQ SPLLGRAPLS AGAWLGAMLA DQSDAPVVMV APTSARAEAL
QREVIYFAQK LTPTLPIHVF PAWETLPFER LSPYGPLVGE RLATLFRIAQ MGGDGPLFSG
DDAGRARALI ITTPAALMQR LMPKKTLLAH GFALAVGDQM DLPRFREFLT RSGYLSVAQV
SEPGEFAVRG GIIDFYPPGA SEPVRVDLFG DEVERLRLFD PVTQRSLDPI PHIEALPVRE
ALLTADAITR FRTNYREAFG GQAAEDEIYR EISQGLPVPG MERYLPMFYD AADDFFDYLP
AGSALLIEEA SWEQVIERER EIIERHQIAS ESGPASRCPE QDALYLSQVE LKERLARFSH
LTLHPEAGEG ENAGFHALPN FHDDEQAKES PGDILARVAK SIDSQARRGR RAVLAVRTVS
QRERLRELLA DHDILTNDAD SWRDALTAPR GAVLLTLGDV AQSFSHPEAE LALITEDAIF
GERIRRRKVD RRYLDQLIAS FSDLAEGDPV VHADHGVGRF GGLHTLKLGE LQNEFLLIRY
ADDDRLYVPV EDLDQVGKHA GGEDVPLDKL GSKRWKRAKK RARKKILEMA QELVALQAQR
ESRPGFQYSG PDALYQEFAA TFPYEETDDQ GAAIEAVLGD MAGPRPMDRL VCGDVGFGKT
EVALRAAFRA AMDGRQVAVL APTTILAHQH YENFAKRLAG YPLKIGSLSR FRTPKEQKTV
VDGLGRGEVD VVVGTHRLLQ KDIKFKDLGL LVVDEEQRFG VTHKERIKQM RADVDILTLT
ATPIPRTLNM AMAGLRDISI IATPPADRLA IRTIVTHYDK QQVREAVLRE LYRGGQVFYL
HNQVSDIDKK AAELGELIPE ARVGVAHGQM KESELERVMM AFYKQTFNIL VCTTIIENGV
DIPTANTIII DRADKFGLAQ LHQLRGRVGR SKHRAYAYLL VPHKRKISND AEKRLAALES
LGDLGAGFML ATHDLEIRGA GNILGDEQSG QIREVGFELY NQMLQEAVEA LKAGKPLPKV
DADDADESDD EQIHPVINLH MSTFIPEAYV PDVHQRLTLY KRIAEMHNAD ELGEMRAELE
DRFGPLPPSV LNLLEVMQIK RQCVALKILK LEAGPKGGSI KFHPEPAIDT AKLLDMIRKG
GGQNRFDAAS HTLGLRNRDW SGERERLQGI REALAALAPN APAKAPRKA
//
