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Database: UniProt
Entry: A0A0U2QMT5_9ALTE
LinkDB: A0A0U2QMT5_9ALTE
Original site: A0A0U2QMT5_9ALTE 
ID   A0A0U2QMT5_9ALTE        Unreviewed;      1157 AA.
AC   A0A0U2QMT5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=AT746_11375 {ECO:0000313|EMBL:ALS98811.1};
OS   Lacimicrobium alkaliphilum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Lacimicrobium.
OX   NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS98811.1, ECO:0000313|Proteomes:UP000068447};
RN   [1] {ECO:0000313|EMBL:ALS98811.1, ECO:0000313|Proteomes:UP000068447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YelD216 {ECO:0000313|EMBL:ALS98811.1,
RC   ECO:0000313|Proteomes:UP000068447};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; CP013650; ALS98811.1; -; Genomic_DNA.
DR   RefSeq; WP_062480396.1; NZ_CP013650.1.
DR   AlphaFoldDB; A0A0U2QMT5; -.
DR   STRING; 1526571.AT746_11375; -.
DR   KEGG; lal:AT746_11375; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000068447; Chromosome.
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:UP000068447}.
FT   DOMAIN          623..784
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          805..959
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1157 AA;  130237 MW;  B289D0DB92D7BBEE CRC64;
     MSSIFSPDLP AKAGDHQQWG NLQGSSLALA IANASERVKG SVLLITADTP SALKLARELQ
     SFVSEIEVKI FPDWETLPYD NFSPHQDIIS QRLETLFHLT QPQPCIYVVP VNTLLQRLAP
     VDYLAKYLLL LEQGQHLDLD SFRQGLERAG YTAVSQVMSH SEFCVRGSII DLFPMGSKTP
     YRIDLFDDEI DSIRIFDPDS QRSEDKVEQI RMLPAHEFPT DKEAIDRFRL QFLDRFDASN
     ARESVYHQVS KGLMPAGIEY YLPLFFEHTA TLFDYLHQDS LVLMHGDLIN AAEFYWADVQ
     ERYEQHKYNP LKPLLSPAEI FLRVEELFNL IKQRARISVG HQSLEPKAGR TNFATTALPD
     IAVKPQLKSP MASLQQQLKV WQQQGVRVLF SVESQGRRES LLEMLKKIQI SPKEVSDLGT
     FLCGHQQLGI VISDLEHSFM LDESDGRLVL ITETELLGHK ISQRRLRKKQ QATDEAAVIR
     NLAELNIGQP VVHLDHGVGR YLGLQTLDAG GIATEYLTIE YANQAKLYVP VSSLHLISRY
     SGGDLDSAPL HHLGTETWAK ARKKAAEKVR DVAAQLLDVY ARRAAKPGFA IKINWDEYES
     FANSFPFEET ADQQQAINAV IQDMGSPIAM DRLVCGDVGF GKTEVAMRAA FLAANGGKQV
     AILVPTTLLA QQHYENFKDR FADWPFRIEV MSRFGSGKEH KEIIQGLNDG KVDIVVGTHK
     LLQDDVKFAE LGLVIIDEEH RFGVRQKEKF KALRADVDIL TLTATPIPRT LNMALSGMRD
     LSIIATAPAK RLAIKTFVRQ RDKQLIREAI MREILRGGQV YFLHNEVETI DKTAAEIEEI
     VPEARVGIGH GQMRERDLER VMSDFYHQRF NVLVCSTIIE TGIDIPSANT IIMDRADHLG
     LAQLHQLRGR VGRSHHQAYA YLLTPHPKRM TKDAHKRLEA IASLEDLGAG FALATHDLEI
     RGAGELLGDD QSGQIATVGF SLYMEMLDKA VEALKEGKEP SLDESLSSHT DIELRIPALL
     PEDYIHDVNI RLSLYKKIAN CKNKDELDDV RVELIDRFGL LPDAAKNLMT IAELKLEAKK
     VGISKIEASS QGGFVEFDQD TPVDPGFIIQ LLQSQPAVYK LDGPQKLRFN IKTEQHQQRV
     TLVQDMLTQF KRKLQAA
//
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