ID A0A1B8PMH4_MORNO Unreviewed; 1197 AA.
AC A0A1B8PMH4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=A9Z60_01360 {ECO:0000313|EMBL:OBX52351.1};
OS Moraxella nonliquefaciens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=478 {ECO:0000313|EMBL:OBX52351.1, ECO:0000313|Proteomes:UP000092671};
RN [1] {ECO:0000313|EMBL:OBX52351.1, ECO:0000313|Proteomes:UP000092671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 60284 {ECO:0000313|EMBL:OBX52351.1,
RC ECO:0000313|Proteomes:UP000092671};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella nonliquefaciens CCUG 60284.";
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:OBX52351.1}.
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DR EMBL; LZDN01000001; OBX52351.1; -; Genomic_DNA.
DR RefSeq; WP_066891030.1; NZ_LZDN01000001.1.
DR AlphaFoldDB; A0A1B8PMH4; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000092671; 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; 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:UP000092671}.
FT DOMAIN 661..822
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 844..997
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1197 AA; 133768 MW; 4F03A3D32CBAD9A8 CRC64;
MININTPIIK PNFHTHFTTQ KDASFALWLS VLSTQNKEHL TLVICPSQSS LQRLSDELDF
FGTSAHVFAD YETLVYDSLS VHQDIISERI DLLTHMPTSG VLLVSVQTLM QKITPPSHLL
GRFFDLNVGD TFDVERERER LAKAGYKVVD NVYMAGEFAV RGSIVDIFAV GQPLPFRLEL
FDDEIETIKF FNPDSQRTIS DEELDTLKKD GVFDDKNAPK SPKVSSFRLL PACEFDLDDK
ERFRQNFSSL FPNVSARKVA FYHDIMNGIQ PPGVEYYAPL FCDLHEWQTY GTLFDYLPKK
TLIVCDDNLS AYHHDFWEQI KARHHSLAFD KDVPILPPDY LYLPSNEFFQ ALKAYPRAVF
GDDREDALTL FDHISTHAVP NLPINHQKDE PLDEFLDFVR VCDEPILLVC ESAGRREIIL
ELLKGKLDGN TVADFDEFLA NLDEYKVTPN NATLPKPSKE ADLDKIALTI APMERGLWLK
SEKNQGICII SETQIFGRAV ATNRHKRQNA LSQALLIKSV SEMTEGSLVV HLSYGIGRYL
GLVVLDVGDG EQEFIHIKYA DDANVYVPIT NLALIGRYSG SDSEAVPLSK IGSGKWDKAR
QKSLTDIYDV AAELLNVQAR RNAKQGISFD IDMASYELFA SGFAYDETPD QQSAIEAVMF
DMKQTKPMDR LICGDVGFGK TEVAMRAAFI AVQAGYQVAL LVPTTLLAGQ HEDSFKDRFA
DWAIKIESLS RFSSKKAQDK VLASLADGKV DIIIGTHRLL QDDVTFKNLG LMIIDEEHRF
GVRHKEKIKA MQAEVDTLTM TATPIPRTLN MALSGMQDIS IIATPPARRL AIKTFVAQKS
EQTTKDAILR EILRGGQVYY LHNDLTSIDT VAQNLSDLIS EVRVGVAHGQ MAHKELHDVM
SDFYHKKTNV LVASTIIETG IDVPNANTII INRADKFGLA QLHQLRGRVG RSHHQAYCYL
FVPSIKGLST DAKKRLDAIS RANTLGAGFM LASEDLEIRG AGEILGKQQS GNMQTIGFGL
YMDMLERATK AIKSGNTPSL ATPLDLVSDI NIHASALIPS DYLADVHERL LCYKRIANAE
TVDELNELRA EMIDRFGAMP TALSNLFLVH KMRVQSMPLG ISKIDVTAFG LSMEFKADTP
VDGLAIVKLI QSNDGYRMNG ATGLKYAFKD EKDVTGRVNA VFELLRYLHG HVAKESE
//
