ID A0A2W5YH86_9MICO Unreviewed; 1201 AA.
AC A0A2W5YH86;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:PZR54261.1};
GN ORFNames=DNL40_04940 {ECO:0000313|EMBL:PZR54261.1};
OS Xylanimonas oleitrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Xylanimonas.
OX NCBI_TaxID=2607479 {ECO:0000313|EMBL:PZR54261.1, ECO:0000313|Proteomes:UP000248783};
RN [1] {ECO:0000313|EMBL:PZR54261.1, ECO:0000313|Proteomes:UP000248783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PW21 {ECO:0000313|EMBL:PZR54261.1,
RC ECO:0000313|Proteomes:UP000248783};
RA Nagkirti P., Shaikh A., Gowdaman V., Engineer A.E., Dagar S.,
RA Dhakephalkar P.K.;
RT "Whole genome sequencing of a novel hydrocarbon degrading bacterial strain,
RT PW21 isolated from oil contaminated produced water sample.";
RL Submitted (JUN-2018) 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:PZR54261.1}.
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DR EMBL; QKWH01000002; PZR54261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W5YH86; -.
DR Proteomes; UP000248783; 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:UP000248783}.
FT DOMAIN 659..820
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 838..995
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1201 AA; 131207 MW; E63ADFCBD1690C46 CRC64;
MNLTGIVPAL LADPGAAAAL EDVRARGFVD VVGPQGVRAP LLVEAARRRP LVVVTATGRQ
ADELAASVRA YLPDEQADDV AVLPSWETLP HERLSPRADT VARRIAVFRR LAHPTPERGQ
AGPVRVLVMP VRALLQPVVD GLGELEPVSL HTGDTADLTD VAERLVGAAY SRVDMVERRG
EFAVRGGILD VFPPTEDHPL RIEFWGDEVS EVRWFSVADQ RSLEIAEQGL WAPPCREILL
TEQVRERARA LTEQLPGAVD MLDRLAAGVA VEGMESLAPV LVDRMVPVLD LVPDDALLVV
DEPERVRRRA HDLVATTEEF LAAAWTGAVA GGQAPIDLSA ASFATFAEVR EIAARRGLGW
WTLSAFGLDP EAEASEAAHG SAGAGPDTTY TVNAREVESY RGDLQRALDD VRRLQKDGWR
LVLTTEGPGP AKRMVEQLMA ADTAARLVAR LDEEPEGGVV LVTPALVGKG FVAPDLRLAV
FSESDLTGRQ GTTTRDMRRL PSRRRNVVDP LQLRAGDYVV HEQHGVGRFV EMVQRTLGAG
ANAATREYLV LEYASSKRGQ PGDRLFVPTD QLDQVTKYVG GEAPSLSKMG GADWKNTKAK
ARKHVKQIAG ELIRLYSARM ATQGHAFGPD TPWQRELEDA FAYVETPDQL STIDEVKADM
EKPVPMDRLV CGDVGYGKTE IAIRAAFKAV QDGKQVAVLV PTTLLVQQHF ETFSERYAGF
PVKVAALSRF QSEKESAETI EGIKDGTVDV VIGTHRLITG SIRFKDLGLV IIDEEQRFGV
EHKETLKQLR TNVDVLAMSA TPIPRTLEMA VTGIREMSTL QTPPEERHPV LTYVGAYEEK
QIAAAVRREL LREGQVFYVH NKVDSIDKTA QRLRELVPEA RVGVAHGKMT ETQLDQIIRA
FWEKELDVLV CTTIIETGID ISNANTLILE RADMLGLSQL HQLRGRVGRG RERAYAYFLY
PPERPLTETA HDRLATMAAH TDLGAGMQIA MKDLEIRGAG NLLGGEQSGH IAGVGFDLYV
RMVGEAVAAY RGDGQEEQPE VTIELPVDAH LPESYIATER LRLEAYKKIA AAADAPALAE
VRAELVDRYG ALPEVASALF DVADFRNHVR RAGLTDVTAQ GKFVRFAPVD LPESAQLRLK
RLYPGTILKP AIRAFLVPFP TTARIGGRPL RGAEVLTWAR QLIDAVVLGD VSAAAGVGTS
R
//
