ID N9K9X4_9GAMM Unreviewed; 1157 AA.
AC N9K9X4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=F909_02081 {ECO:0000313|EMBL:ENW80793.1};
OS Acinetobacter sp. ANC 3929.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217707 {ECO:0000313|EMBL:ENW80793.1, ECO:0000313|Proteomes:UP000013159};
RN [1] {ECO:0000313|EMBL:ENW80793.1, ECO:0000313|Proteomes:UP000013159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3929 {ECO:0000313|EMBL:ENW80793.1,
RC ECO:0000313|Proteomes:UP000013159};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. ANC 3929.";
RL Submitted (FEB-2013) 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:ENW80793.1}.
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DR EMBL; APRH01000022; ENW80793.1; -; Genomic_DNA.
DR AlphaFoldDB; N9K9X4; -.
DR PATRIC; fig|1217707.3.peg.2022; -.
DR HOGENOM; CLU_005122_0_3_6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000013159; 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; 3.40.50.11140; -; 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; 3.
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}.
FT DOMAIN 624..785
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 806..960
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1157 AA; 131205 MW; EB8EDDE30B9741F3 CRC64;
MIFSMFQQEI SQLNLQQFKA GEKRWIGSLL GSSAALLFKE IATQSTNLYV IVARNNQHLA
QLESELEFYG IKPVIFPDWE ILPYDRLSPH QDIVSERLAI LSNMPQKGIL LVSASTLGQR
VAPYSWVVGE HFDIKVGQKL DLEVQKKQLV QAGYRLVDTV YDHGEFAVRG SIMDIYASGQ
DQPIRIDLFD DEIESLKFFD PETQRTTESL KNFTVLPAKE FPLKEGRSTF RDRYAESFPT
ANPKKNPIYQ DVLDGIPTPG LEFYLPLFFE KKVMEAQSML TTYLPNNCVV ITNNEIENDL
INFWKEVVRR YEDRRHNIDQ PILPPEELFL MPNHVLQALN QFPRILTSAE VYDDKAGVLN
IKAEQPPKLA VDPKKEQPFA AVKHYIDQVK HPVLLVAESA GRRETLKDAL RSILGDIQNV
ESFAQFQKEQ LQIAITSAPL DRGLLLTNQL SVISENQLYE HRVVQRRRKR QQEVSEEFLV
RSLTELSIGA PVVHIDHGVG RYAGLITLEI DQQDHEFLQL DYADGAKVYV PVTNLHLISR
YSGGDPDLAP LHKLGTDTWS KAKRKALEQI HDVAAELLHI QARRQSKPGF AFELDHTGYM
QFASGFAYEE TLDQANAIDA TLHDMQLAKP MDRLVCGDVG FGKTEVAMRA AYVAVQNNKQ
VAVLVPTTLL AQQHYESFKD RFADTAVRIE VLSRFGSNKT HLKIIEDLAD GKVDIVVGTH
KILQENIQFK NLGLMIVDEE HRFGVRDKER IKALRADVDM LTLTATPIPR TLNMAFSGMR
DLSIIATPPA RRLAVKTFVQ EHTDDSVKEA ILRELLRGGQ VYLLHNEVDT IERAAETIRN
LVPEARVAVA HGQMRERELE QIMQQFYHKE YNVLVCSTII ETGIDVPNAN TIIIERADKL
GLAQLHQLRG RVGRSHHQAY AYLLVPSLKH LKGDAEKRLD AIQRASTLGA GFMLATEDLE
IRGAGELLGE QQSGSMQAIG YSLYMEMLEK ATKAIQKGKT PNFDAPLSLT AEINLHMPAL
IPDDYLGDVH QRLLFYKRIS GTDSQEKLDN IRMELIDRFG IPPQPVKQLF SVHQLRLRAE
QLGITKIDIN SNGGYIEFAP DTPVQALSII QLMQKNPTYY RMEGGQRLKV MVQLAEYDKR
IQFIVDLLNK LLSELDR
//
