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Database: UniProt
Entry: A0A084A6T8_9GAMM
LinkDB: A0A084A6T8_9GAMM
Original site: A0A084A6T8_9GAMM 
ID   A0A084A6T8_9GAMM        Unreviewed;      1159 AA.
AC   A0A084A6T8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   ECO:0000313|EMBL:KEY61017.1};
GN   ORFNames=SRDD_00140 {ECO:0000313|EMBL:KEY61017.1};
OS   Serratia sp. DD3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY61017.1, ECO:0000313|Proteomes:UP000017810};
RN   [1] {ECO:0000313|EMBL:KEY61017.1, ECO:0000313|Proteomes:UP000017810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD3 {ECO:0000313|EMBL:KEY61017.1,
RC   ECO:0000313|Proteomes:UP000017810};
RX   PubMed=25212623;
RA   Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT   of Daphnia magna.";
RL   Genome Announc. 2:e00903-14(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:KEY61017.1}.
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DR   EMBL; AYKS02000002; KEY61017.1; -; Genomic_DNA.
DR   RefSeq; WP_023491792.1; NZ_AYKS02000002.1.
DR   AlphaFoldDB; A0A084A6T8; -.
DR   STRING; 1410619.SRDD_00140; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000017810; 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:UP000017810}.
FT   DOMAIN          625..786
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          808..961
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1159 AA;  131075 MW;  FAE455DF6982CEE7 CRC64;
     MSTSDNSRRS ALSSARYPLP VRAGDLRQLG QLTGSACAVE CAEITERHSG PVLLIAPDMQ
     NALRLRDEIQ QFTDQMVTTL SDWETLPYDS FSPHQEIISS RLSRLYHLPA MESGIIILPV
     NTLMQRVCPH EFLRGHALVM KKGQRLSRDL LRTQLEQAGY RCVDQVMEHG EFATRGALLD
     LFPMGSDAPF RIDFFDDEID SLRTFDVDSQ RTLSEVESIN LLPAHEFPTD KNAIELFRSQ
     WREQFEVRRD AEHIYQQVSK GTWPAGIEYW QPLFFSQPLV SLFSYLPANT LVVNTGDLES
     AAERFWQDVN QRYEGRRIDP MRPLLPPETL WLRVDALFGE LKAWPRIALK PEELPDKAGC
     CNLGYQPLPD LAVQAQHKSP LDNLRRFIEH FTGSTVFSVE SEGRRETLQE LLGRIKLNPP
     VIQRLDELNA TGSYLMVGAA ERGFIDTLRN RAMICESDLL GERVSNRRRD NRRTINTDTL
     IRNLAELHPG QPVVHLEHGV GRYVGMTTLE AGGIKAEYLI LAYSGEDKLY VPVSSLHLIN
     RYAGGADDNA PLHKLGSDVW SRARQKAAER VRDVAAELLD IYSQRAAKSG FAFKHDREQY
     QLFCQTFPFE TTPDQEQAIN AVLSDMCQPL AMDRLVCGDV GFGKTEVAMR AAFLAVENGK
     QVAVLVPTTL LAQQHFDNFR DRFANWPFRI EMMSRFRSAK EQQHTLQEAV EGKVDIIIGT
     HKLLQSDLRW KDLGLLVVDE EHRFGVRHKE RIKAMRADVD ILTLTATPIP RTLNMAMSGM
     RDLSIIATPP ARRLAVKTFV REYDSLVVRE AILREVLRGG QVYYLHNDVD SIDKAAQRLA
     ELVPEARIAI GHGQMRERDL ERVMNDFHHQ RFNVLVCTTI IETGIDIPSA NTIVIERADR
     FGLAQLHQLR GRVGRSHHQA YAYLLTPNPK VMSTDAHKRL EAIASLEDLG AGFALATHDL
     EIRGAGELLG EEQSGQMTTV GFSLYMELLE SAVDALKNGR EPSLEDLTSQ QSEVELRMPT
     LLPDDFIPDV NTRLSFYKRI ASAKNEGELE ELKVELIDRF GLLPDAARNL LQSAAMRQQA
     LKLGIKRIEG NERGGFIEFG DKNQVDPGYL IGLLQSKPPV YRLDGPTKLK FTLDLSDRLK
     RLTFIAELLV AFREHTLAA
//
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