ID A0A199NV63_9MICC Unreviewed; 1209 AA.
AC A0A199NV63;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AN277_0200845 {ECO:0000313|EMBL:OAX52944.1};
OS Rothia kristinae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX52944.1, ECO:0000313|Proteomes:UP000053171};
RN [1] {ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S., Matcher G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAX52944.1, ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA Dorrington R.A.;
RT "Identification of putative biosynthetic pathways for the production of
RT bioactive secondary metabolites by the marine actinomycete Kocuria
RT kristinae RUTW2-3.";
RL Submitted (JUN-2016) 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:OAX52944.1}.
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DR EMBL; LJBJ02000001; OAX52944.1; -; Genomic_DNA.
DR RefSeq; WP_055684368.1; NZ_LJBJ02000001.1.
DR AlphaFoldDB; A0A199NV63; -.
DR Proteomes; UP000053171; 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:UP000053171}.
FT DOMAIN 675..836
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 861..1011
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1209 AA; 131778 MW; 6D3A00175802C089 CRC64;
MSLTGLRTAL SQESTFANVL RQASVPAAQR SAETVIGAAE GLRAPLVAQI SDGLAAADAA
SGRADGHAPV VLAVTATDRE AEDLEAVLGS YLPEEAVTRF PAWETLPHER LSPRSDTVGQ
RLAVLRRLAE ERDGTRVVIA PIRSVLQPIA ASLDAMRPVR LAVGEERDFE QTVQALSDAA
YSRVDLVTRR GEFAVRGGIL DVFSPVEDHP VRIEFFGDEV EQMRWFAVAD QRTFTPQHGR
DPQELIAPPC REILITPAVM SRAAKLKDSL PGEESMLERI AGGIYVEGME SLAPLLVDAM
TTLVASLPAG SLAVLCEPER IRTRAADLVA TNQEFLLAAW EQASDGQAAP IDLQETGLAA
GSFMDVAEAR AQALEAGIGW WAITSLGVDE AIEDDADTLT IAVRAPLTFA GDVQALLDVV
AQHVREQWQV VAVTEGPGPL KRLAELFREA DLPAAIHEDL TEPPAPGVIA LTTAAHGTGF
VLEEAKIAFL TEADVLGRAS PYTTRDMRKL PAKRRRNAVD PLALKAGDYV VHEQHGIGRF
VELIQRPIAG AMVKPGQPKP MKEYLVLEYA AAKRGAPKDR LFVPTDQLDQ VTNYVGGDAP
TLSKMGGSDW AKTKSRARRA VKEIAADLIR LYSARMASRG HAFAPDTPWQ RELEDAFPYI
ETPDQLTTIN EVKADMEKET PMDRLISGDV GYGKTEVAVR AAFKAVQDGK QVAILVPTTL
LAQQHTETFT ERFSGFPVRV ATLSRFQTPK ESQAVEAGIA DGSVDVVIGT HRLLSQAVKF
KDLGLVIIDE EQRFGVEHKE KLKTLRTNVD VLAMSATPIP RTLEMSLTGI RETSTLATPP
EERHPVLTFV GPSTDQQVAA AIRRELMREG QVFFVHNRVS SIDRTAADLQ RLVPEARIAV
AHGQMSEARL EQIIVDFWEK RFDVLVCTTI VETGLDISNA NTLIVDRADH YGLSQLHQLR
GRVGRGRERA YAYFLYPPEK PLGEVALERL KAVAAHNELG AGMQLAMKDL EIRGAGNLLG
GEQSGHIAGV GFDLYLRLVG EAVADFRGEK EEAAPAEMKI ELPVDAHLPH DYVPGERLRL
EAYRNLAAAA TDEAVDEVAA ELADRYGELP EPARNLLAIA RLRIRARAAG LSEIMTMGSK
IRFHPVDLPD SRRMRLERMY PGALVKPVPG TEIRQILVPK PKTAPVGGKD LVDGQILAWV
REFIDAILA
//
