ID D8TU12_VOLCA Unreviewed; 1119 AA.
AC D8TU12;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=VOLCADRAFT_90307 {ECO:0000313|EMBL:EFJ48957.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ48957.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC {ECO:0000256|ARBA:ARBA00025673}.
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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000256|ARBA:ARBA00006637}.
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DR EMBL; GL378337; EFJ48957.1; -; Genomic_DNA.
DR RefSeq; XP_002949854.1; XM_002949808.1.
DR AlphaFoldDB; D8TU12; -.
DR STRING; 3068.D8TU12; -.
DR GeneID; 9619206; -.
DR KEGG; vcn:VOLCADRAFT_90307; -.
DR eggNOG; KOG1123; Eukaryota.
DR InParanoid; D8TU12; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd18029; DEXHc_XPB; 1.
DR CDD; cd18789; SF2_C_XPB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR NCBIfam; TIGR00603; rad25; 1.
DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR PRINTS; PR00851; XRODRMPGMNTB.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058}.
FT DOMAIN 663..825
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 866..1025
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 118846 MW; 49018752F6A266B7 CRC64;
MKGMASSPRD LGHHTEAVVP GPRQTPAITV TGRLKRPRPA DQPAAAANPD EALEDLEDRD
QSPDRDAVAS ALQGRGAVVA AAAGAQKPPG ARPGLDVEDD DEEDAGLRRG RKVRKTARMI
QDEDDDDEEM DAARSQRSTG SGGVDVGLRG SAMRGGAGVG AGAAPPAAAA AAAAAQRPGV
AAGRAGGAVS MSVSPPSRGS TSPSGSSGAY GQPANSNRTR AVAAAAAAAA AAAARAGKPP
AGAAGPGGWK PATAPTPTPA PAAAPATKSA APNAGAAAPT AAAGRGSRSR KPTKQFGAEN
DGEELSDDPF DKEEEAEFKL VTDDDDDGDY DDDDDLGGRR RGGWKRRGGF GAGGSSGRPG
GGRGGFFGNR IFLETFSPIY KQVKGGKEGL KGVEHRRGLG LAYDFLIAIS EPVCRPEAMH
EYQLTPHSLY AAVSVGLETE TIINVLNRLV GLSKVQLSEE TKSFIRDSTA NYGKVKLVLK
HNRFYVESTH PEVLKRLLKD KVIQEAAVGG GIIQSSRALR EHAAANITTA VDMVGEEAPP
QEPQKPEKGL GDEAGKTAPG GFGGGDGKGG SAAGEVVADG EEDDGVGAYG KAFKDISAEE
TEQEVQEFEV EEVKKRCMPE GLNYPMLEEY DFRNDRRNPD LLPFELKPHV KLRPYQEKSL
SKMFGNGRAR SGIIVLPCGA GKSLVGVAAA SRVKKSCLCL CTSSVSVDQW KYQFQLWTSI
GDHQIARFTS ENKEMFPGEV GVLVTTFTMI AFSGKRSEES ERIMNCIRSR EWGLLLMDEV
HVVPAQMFRT VISTCKSHCK LGLTATLVRE DERIADLNFL IGPKLYEANW LDLTRAGHIA
NVQCAEVWCP MTGEFYREYL KKENGPRRQL LYCMNPNKII VFSDNIWALR EYATRMRKPF
IYGPTSHAER TRVLHAFKHN PDINTVFLSK VGDNSLDIPE ANVLIQISSH AGSRRQEAQR
LGRILRAKKG MGGGPDGEEM YYSTKRQQFL IDQGYSFKVV TNLLDAAAGS AGLMYSDKSS
QLDLLSRVLS AGMEEAGVET LRDEDAEGLA AAAGQRPAAR RRVGDMAALT GASGIRYLEF
ASGGVGRGGG GGGGRGGRAG YQGAKAQSWA RKLGIAAKR
//
