ID K1XTH3_MARBU Unreviewed; 1010 AA.
AC K1XTH3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=MBM_05865 {ECO:0000313|EMBL:EKD15854.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15854.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD15854.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15854.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; JH921440; EKD15854.1; -; Genomic_DNA.
DR RefSeq; XP_007293754.1; XM_007293692.1.
DR AlphaFoldDB; K1XTH3; -.
DR STRING; 1072389.K1XTH3; -.
DR GeneID; 18761800; -.
DR KEGG; mbe:MBM_05865; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_004585_4_2_1; -.
DR InParanoid; K1XTH3; -.
DR OMA; DYPDATT; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 8..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 285..594
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 694..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1010 AA; 112375 MW; 9EF6969E9462862A CRC64;
MNPDGLLTNL NQSQQAAVSS FADTLAILAG PGSGKTHTLT SRTAWLLAQG LQPWNVIVAT
FTVKAAREMK ERIGKLIGNG TESKLILGTF HSIARRYLAR YGHLIDIKKD FGIADSADSL
AIIKRIVKRH RFMIDAKVVR SRISGLKART SVDQEVKSQK KFGAKIVEEQ EFEKCYEEYE
EALRRSNLLD YDDLLLRCVD LLRMHPSCVS NVEAVLIDEF QDTNLVQFDL MRLFAAQRKR
ITIVGDPDQS IYGFRAAEIK NYKRMLHQYP DTVTIALEEN YRSSGAILMS ALSVIQQDSS
RVAKSLLATH SPGTRPVLRK LSGAQKEAHW IVTEIQRIRG MTGELLDLND FAILLRSSAL
SRLIETALGK AGIAYRMVGG QRFYDRLEIK TVLDYLRVIN QPDNNDALAR IINTPSRRIG
EATIKDLLEE ADQSKITLWT LILNIVQRKR TTKTKLKNKQ EQNLAAFVNI ILMGRSKSAG
PPDERLSTSG LIQFVLAKTS YERWLEEHHG DENKARWDNV QELITQANDF EDLISFGYED
ETLPEIDGLK QNDDADTLSR FLANVALASE VKPEDAETAT ITRITISTIH AAKGLEWPVV
FIPAAYQGSI PHSRAEDTNE ERRLLYVAMT RAKALLYMSC PIKSTSNEDT ILSPFLTPPG
LASLLDAKGP SLGSPAVTDL AQILRRNLPS RRSIEKSSAS LTSTEDDLFP ERGEEKESDQ
ELRWNSMTAG TSSFMAGQQA PKRRRAELGR SMSNLEGPER DWKPSYATTM DRAASFTTAG
FVTAGSHLQV LKEQSVNGTL NDEQDAEDFD RGKKKPKQTG RLPEGQGTLF GFFGKSEPQV
NKPVPMIKET DPKPRAPIVA KSFNQARSKS TTSEHVGIAT ALSNHRLGNG TSGNRLRQNA
QLDVQSHRND YVFLSSSPPR PNPPSPTHQE KKLSPQPPPQ PAGLTARPPI LNKIRPPIIS
THQTTVSMLQ NGNVNGTGAR KTLGVRRSMD GWASRKGQKQ SFKPPTMQRP
//
