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Database: UniProt
Entry: A0A0S9R5C5_9ACTN
LinkDB: A0A0S9R5C5_9ACTN
Original site: A0A0S9R5C5_9ACTN 
ID   A0A0S9R5C5_9ACTN        Unreviewed;      1161 AA.
AC   A0A0S9R5C5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=ASF37_12050 {ECO:0000313|EMBL:KQP77281.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP77281.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
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:KQP77281.1}.
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DR   EMBL; LMNK01000003; KQP77281.1; -; Genomic_DNA.
DR   RefSeq; WP_056552430.1; NZ_LMNK01000003.1.
DR   AlphaFoldDB; A0A0S9R5C5; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051640; 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:UP000051640}.
FT   DOMAIN          629..790
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          808..965
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1161 AA;  126305 MW;  23197EDEA3686897 CRC64;
     MDLHALLSPH LAGSLADVVS QRPRTVTLQG PAALRPFVAR AAADASTVLA VTPTAREADE
     LAADLSVLLG DDAVVVYPAW ETLPHERLSP RSDTVGRRLA VLRRLAHPGA GAPPVRVVVA
     PVRSILQPQV AGLADLTPVE LVVGQQAPLD DVVRDLAAAA YVRVDLVERR GEFAVRGGIV
     DVFPPTEDHP LRIDFWGDEV EEIRWFSVAD QRTTDAVERL WAPPCRELLL TDEVRGRAAA
     LATEHPALAE LFGKVAEGHA VEGMESLAPV LVDELELLVE VLPSDAVVVV NDPEKVRARA
     ADLNATNEEF LQASWAAAAT GAAAPIDLGA AAFKELEEVR AVALARGLAW WNLSPFGLDD
     EDTVVVPAEA APLYRGDTEQ AVADVRGWLA DGRFVVVAAP AAGQAQRTVE WLAEHDVPAA
     LVDGDTPAPE AGSGVVAVLV ADVDHGLVAA KAVLLTHDDL VAQRAAERPD RSSMPVRRRK
     QVDPLELKAG DHVVHEQHGV GRYVELVNRT IQGAAREYLV IEYAPSKRGQ PGDRLFVPMD
     QLDLVSRYVG GESPSLDKLG GADWTARKNK ARKAVRQIAG ELIKLYAARQ STKGHAFGPD
     TPWQAELEDA FAFVETPDQL ITIDEVKRDM ERQVPMDRLV CGDVGYGKTE IAVRAAFKAI
     QDGKQVILLV PTTLLVQQHY ATFAERFGQF PVTIKPLSRF QTEKESQATL DGLADGSVDL
     VVGTHRLLQP GVRIKDLGLV IVDEEQRFGV EHKEALKHLR AAVDVLAMSA TPIPRTLEMA
     VTGIREMSTI ATPPEERHPV LSFVGAYDDK QVAAAIRREL LREGQAFFIH NRVQSIDKVV
     RRLGELVPEA RIAAAHGQMG EHQLEKVMVD FWEKRYDVLV CTTIVESGLD VSNANTMIIE
     RSDTLGLSQL HQLRGRVGRG RERAYAYFLY PPDKPLTETA HDRLATIAQH SELGGGMQVA
     MKDLEIRGAG NLLGGEQSGH IADVGFDLYV RLVGEAVAEF RGEGEAGPQG AREVKLELPV
     EAHLPHDYVP SERLRLEMYK RLADVRSLDD VAELRAELVD RYGEPPEVAE VLLDVARLRV
     AVRAAGLTEV TSAGSQIRFG GLSLPESAQM RLRRVYPKSI YKPATDVALV PAPRTAPVGG
     RPLRGRELLE WVDTVVQTLV A
//
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