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Database: UniProt
Entry: A0A094J9S4_9GAMM
LinkDB: A0A094J9S4_9GAMM
Original site: A0A094J9S4_9GAMM 
ID   A0A094J9S4_9GAMM        Unreviewed;      1155 AA.
AC   A0A094J9S4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=HR45_18925 {ECO:0000313|EMBL:KFZ35987.1};
OS   Shewanella mangrovi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ35987.1, ECO:0000313|Proteomes:UP000029264};
RN   [1] {ECO:0000313|EMBL:KFZ35987.1, ECO:0000313|Proteomes:UP000029264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YQH10 {ECO:0000313|EMBL:KFZ35987.1,
RC   ECO:0000313|Proteomes:UP000029264};
RA   Liu Y., Zeng R.;
RT   "Shewanella sp. YQH10.";
RL   Submitted (JUN-2014) 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:KFZ35987.1}.
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DR   EMBL; JPEO01000028; KFZ35987.1; -; Genomic_DNA.
DR   RefSeq; WP_037445760.1; NZ_JPEO01000028.1.
DR   AlphaFoldDB; A0A094J9S4; -.
DR   STRING; 1515746.HR45_18925; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000029264; 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; 3.40.50.11140; -; 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:UP000029264}.
FT   DOMAIN          619..780
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          789..955
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1155 AA;  129798 MW;  8745CEDBA193E468 CRC64;
     MTVFSVLAPP SATQAGDVRF LNVPEGVARA LTLAELAKAH DGISLLITPD TPSAMTLEAE
     LRYLLGDSLP VWLFPDRETL PFDSFSPHQD LISQRLETLS RLPTANKGLL IVPVSTLMVR
     LPPKAFMSAN VMLLKKDDKY PLEQMRQYLV DAGYHNVGQV YEHGEFAIRG SIIDIYPMGS
     NEPLRIELFD DEVESIRFFE ADSQLSKAPV NEIRMLPARE FPTDDAAIEG FRLRYRRYFE
     VVVKEPESVY QQVSRHILPA GIENYLPFFF DETATLFDYL TPAVQLLTVG DLSSAADEHL
     KQVQQRYEDR RVDPLRPLLA PQDLYLLNEQ LFSELKARPR VQLSSSEQKH QLTAALQPLP
     DLSINHKLRQ PLATLEEYLV GASGRVLFSA ESEGRREALL ELLSKINVKP NRFANAADFF
     NAKDAIGLIV SPLSQGCRLA DPDISIICET ELFGARISQQ RRRDKQRQVS QDALIRDLAE
     LKVGQAIVHI EHGVALYQGL ETLDTGGMVA EYLKLEYAGG DKLYVPVSSL HLISRYTTGP
     EEDPALNKLG NESWAKARKK AIERIRDVAA ELLDVYARRQ ARPGFACELD DTEYAQFAQS
     FPFEETVDQE NAIEAVLGDM QSATAMDRLV CGDVGFGKTE VAMRAAFVAV NAGKQVVVLV
     PTTLLAQQHF ENFKDRFADW PVRIEVMSRF RTAKEQSQVL DALAEGKVDI VIGTHKLLNS
     EVKFEDLGLL IIDEEHRFGV RQKEKIKALR ANVDILTLTA TPIPRTLNMA MSGMRDLSII
     ATPPAKRLAV KTFVREYDKN TIREAVQREI LRGGQVYYLH NNVESIERAA EELRELVPEA
     RVVVAHGQMR ERELERVMSD FYHRRYNVLV CTTIIETGID VPSANTIVIE RADNFGLAQL
     HQLRGRVGRS HHQAYAYLMT PHPKCMTSDA RKRLEAIDAL EDLGAGFMLA TQDLEIRGAG
     ELLGEEQSGH ISKIGFSLYM EMLESAVKAL KQGKEPSLAQ MLNEQCEMEL RIPALLPEDY
     VGDVNIRLSL YKRIANCHTE AALDELKVEL IDRFGMLPEP TKNLMEMTLL KHQATLLGIK
     KLEMHSRGGS LEFNDDHVVD PGFIIGLLQS QPQIYRMDGP NKLKFAMAME SSKQRLDSAQ
     LLLTQLAQHR VGDQA
//
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