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Database: UniProt
Entry: A0A0Q5CFA2_9MICO
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ID   A0A0Q5CFA2_9MICO        Unreviewed;      1207 AA.
AC   A0A0Q5CFA2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ASF54_12220 {ECO:0000313|EMBL:KQQ26726.1};
OS   Frondihabitans sp. Leaf304.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ26726.1, ECO:0000313|Proteomes:UP000051456};
RN   [1] {ECO:0000313|EMBL:KQQ26726.1, ECO:0000313|Proteomes:UP000051456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ26726.1,
RC   ECO:0000313|Proteomes:UP000051456};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ26726.1, ECO:0000313|Proteomes:UP000051456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ26726.1,
RC   ECO:0000313|Proteomes:UP000051456};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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}.
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:KQQ26726.1}.
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DR   EMBL; LMNV01000003; KQQ26726.1; -; Genomic_DNA.
DR   RefSeq; WP_055963286.1; NZ_LMNV01000003.1.
DR   AlphaFoldDB; A0A0Q5CFA2; -.
DR   STRING; 1736329.ASF54_12220; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051456; 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; 3.40.50.11180; -; 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; 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; 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:UP000051456}.
FT   DOMAIN          663..824
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          849..999
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1207 AA;  131438 MW;  85F392E577FA839F CRC64;
     MILQGLIPAL SRASTFDSAL KQATRSSDFS LVDGLRVPLL AGLLDRRAEG SGAAQALLVI
     TATGRESEAV RTSLTSYLPG AEVIEFPAWE TLPHERLSPS AETVGKRIHA LRRLVEWQSA
     FASDPSSVAP LVVVAGVRAA LQPISDNLTD IDAVRLTVGE RGYDLSAIAV RLVDLAYARV
     DMVTRRGEFA VRGGILDVFP PMAEHPVRVD FFGDEIDQIR LFAVADQRSL DTEAKTVELP
     PSREMLLTES VRQRAREMQH EFPSLAQMLE KIGQGIPVDG MESLAPALVH RLVPLTHYLP
     PSAAIAVLSP ERVVSRAKSL ADTNREFLQA AWSAATAGAE APIDLDSGDF LTVGDLRLQA
     GDRTWWSLSG FDSGVVLSDE ERIESAGDYV RIDAETVPSF SGNAEGAVEH VAELAAAGWS
     IVVTARGVGL VDRARDVLAE RGVAARIVEA LGDDLEPGVV HLVTGGVEAG FQVPEAKLAV
     LGEADFFGRA AGYDGRQVKK LASRRKNVVD PLQLKTGDIV VHSTHGIGRF LELTSREVSS
     GGRNAVKHSR EYLVLEYAPS KRGQTGDRLY VPTDQLDLLS RYVGGEAPKL SKMGGSDWSQ
     AKGKARKAVR DIAVELVKLY SARMASRGHA FGPDTPWQRE LEEAFPFAET PDQLTTIDEI
     KADMERPIPM DRLISGDVGY GKTEVAIRAA FKAIQDGKQV AMLVPTTLLV KQHMETFSER
     FAGFPVHLRA LSRFQTAKES KETIKGIGDG TVDIVIGTHR ILTEGLSFKD LGLVIIDEEQ
     RFGVEHKDQL KKLKTNVDIL AMSATPIPRT LEMAVTGIRE MSTLATPPED RHPILTFVGP
     NSERQIGAAI RRELLREGQI FFVHNRVSSI NRVAAQLAEL VPEARVAIAH GQMPESALEQ
     VMVDFWERKF DVLVSTTIIE TGLDIANANT LIIDRADRYG LSQLHQLRGR VGRGRERGYA
     YFLYDADKPL SETAQDRLET IAANNELGAG MQVALKDLEI RGAGNLLGGE QSGHIAGVGF
     DLYLRMIGEA VNAFRGDVAE GQTELRLELP VDAHIPEDYV ESERLRLEAY QKLSTASSPT
     SSDEQIDSVL EELTDRYGEP PAEVLALIEV SRLRRMAQKT GLSEVVAMGT NMRVAAMELA
     DSVQLRLARL FPGARYFAQT KSVSVPMPRK NGEALPDAEL ITWVEQLLTS VYGAEPARPA
     DSAAAPS
//
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