ID D8TKQ2_VOLCA Unreviewed; 2539 AA.
AC D8TKQ2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ52104.1};
GN ORFNames=VOLCADRAFT_120343 {ECO:0000313|EMBL:EFJ52104.1};
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:EFJ52104.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GL378325; EFJ52104.1; -; Genomic_DNA.
DR RefSeq; XP_002946878.1; XM_002946832.1.
DR STRING; 3068.D8TKQ2; -.
DR GeneID; 9618236; -.
DR KEGG; vcn:VOLCADRAFT_120343; -.
DR eggNOG; KOG0384; Eukaryota.
DR eggNOG; KOG3762; Eukaryota.
DR InParanoid; D8TKQ2; -.
DR OrthoDB; 316826at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR024989; MFS_assoc_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12832; MFS_1_like; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 355..426
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 451..550
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 591..765
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 856..1025
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 128..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2035..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2109..2539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..448
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 132..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1832
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1834..1848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1849..1878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1985..2010
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2117..2138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2188..2238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2251..2385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2517..2539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2539 AA; 272439 MW; B1D098BC4581189E CRC64;
MGATGTLMGL TLTITCAAEV PAFQLQDRLL DSWGVPAVLD LVQAVYVVRL ALYAALPYAG
NVMWVLPVEV LHGITFACGW GAGTVNCKLL APPEMAATLQ GAFQGLYFGL GYGLGSLVGG
WQGTKLGWQD DDDDNGADDD DDDDDDDDDA SEEAPPRRRK AAAPARTRAR RSTRSSKSYK
DESDEDVDMN DDDDEEEEEE EDDDDDDAGD DDEDDDEDEE DGGDEDDDDE EDYAPRKRRS
RAMSASAAAR PRRQAAQQAK ARLRQDSVED DDEEIARAID RQINGLRARP RRVRVCVLTR
VAKVVSYAES DDDDDDDEGG GGGGGGRGGG RGGGGGKAKE ALSAFEDPDE DEVEDEIDKV
LAHRESETLS PVAGDPWASR EFYIKWKRYS YIHCSWDSRA VLEHLRGYKR VLIYIKRVDD
VEEGRRGFSR EEQEMQDVER EMEAQLNQQH MQVERVLAEK QACVYCSPPD EKEDEAEGAR
GSVGPPGQRR RELEAADVEM VNVTKYLVKW EGLPYAECTW ETVNDVIKAG GSTQIDLYLQ
REQRLLEPGR SVDVARKQFK IKGTRALEKQ PEYLRGGTLR DYQMESLNWM IYSWSENRNI
ILADEMGLGK TVQCVSFVGY LAEALQIRGP FLVVVPLSTV PNWIREFRRW VPFVNAVVYV
GDSRSREVLR AYECDPASHH KSSRPHKFEV LLTTYELILK DAQILSRIKW AYLLVDEAHR
LKNAESALYQ ELMEWHFKNK LLVTGTPLQN SLKELWALLH FLDPDKFPTC ERFEAEYSLE
TADSVSGLHG VLRPHLLRRV IKDVEKSLPP KNERILRVDM TPLQKQYYKW ILTRNFKELN
KGSLGSHGGG HVSLLNIIGE LKKCCNHPFL FESAEENYRG SEDDKSAMVR VLDIISDYMR
HRGFTHQRLD GSTPAAARHA AMEHFNRPES PDFAFLLSTR AGGLGINLAT ADTVIIFDSD
WNPQNDLQAM SRAHRIGQTE TVNIYRFVTS GSVEEDILER AKRKMVLDHL AGASAKQMFG
KDELAAILRF GAEDLFKQAP EDDSNAAERV RSALYEDDID AILERAEVVD TRALAAAGAE
ENAAAAAELL SSFNVATFKN EEDDAAFWSK LIPPSERPKE EEEDLLPRSA RRALAADSDD
DNGGGGGAGG GGAGGPGGLG GRRAGGGAGG GGRGGRGGGG ARGGGGGRSK PGAASGGLEP
GPPVDGAALR VDEWIVEVDK EGIPLMKLLQ HLNPPSPTNK VTNQPANEPQ EDGSEPESRS
LSRRDAAAFV RAVRRYGRRE RLADVASEVG RSLEESSAGQ RLSLWHSLMD GCRAAVQRTT
EELKEDAKGV QDAILDFFGV SVKAAELLAV CSCLRLLAKK VAAAREPAVQ HFRLDATSQL
TVPKWGKTIN WTSREDALLL LGVHLYGMGH WDRVAADEAL RPHLADKLAG AVGGAAAARE
RERDDAAAGK DGMGIGLPKA SHLETRALGL LRKMHAVHKA ATAPPVRRPA AGAAARKKGI
AAAAVAAAAG GSGGGGAGGA QAPVHPPPPH DRDGGRADGA TAAGVVPGPV RERERELPPA
LAPPAAAAPA AGRDPCAVGV VNGAAAASAP GGAAAGGGAG GGAGGHAAGG KRKAGGGSVA
AADAAAPGGA AAAAGPSEKR PRMDARVGVS AEPKAVTTAA NTAAAAPAAD GPVGREELKT
LLEPAMSDIR KLRKLQDGSI TDKSVIVQNT KLYLTAIGGH IERVMSVRGP NVSKKLWDLA
ARNIGNGKTG AELRQLHTRI QQSQQQQQSA QPQPQKHQQQ QKPPPPHSGQ VELRSPRHER
EAAAAATQGG PGLRSPKPKP KASPPAVPSA APPLSQRPSA SRSVAVSTTP LPPLPPLSGT
AAAAHPSPPP PPHPPQGYQA SRRHPSEPLA TSHHAVVAAA AAAVAPAGPT MHHRQHSASP
PGPASPLSPP PPALPPPMPP PAAPPPPAPP PLPPMPPPAP PPPLPLPIPP PAPPPGGPPP
LHPSYHPHLH RHPHHHHQHL HAHHHNFNHL HPPTSRVPPP QLLLPGDMAI QFPGLGSGLS
SQAGEPSSGG DLCHVSPPGP CFGAGGGAVS PPVTRWPPEL SPTAIAVAAP SASTAVGTTA
VAGVDMPQEL GFHTLPPSLP PQQPAPQPPP PPQQQQPQIA SPPGLRDAVG GSGGECGGME
LSPRDCRGGG VSAGGQPPPP PQRNSAEAPD TRWDRDPRDP RDRDRGRDRD RDRDPRDGRG
SDPGRSAHHE DRDRDRGGGS SGGGGGNGGG AREWRERERD RRTSRSRSRE RERERDFRSR
EYDRDRDGRD PPRDRRDRDV RDRDRDQRRD PRDRDWDRDR DRDRDTARGR DNRDHREFDR
DRDRGRPLRG AHYEDRGRDY GGDRARDVRD RSRERERERR DRSRSRSRDR RCRSRSRSRG
RERGRGERER DRIRRSRSTS RDRFDRERER ERDEPAGRSG GGGGNGLSRG ASFGPTGGGG
GHGGLAGGGP GLRGGGGSSG GALAAGALAS GPTPLGDNAS VPPGSHLGGG GVAAAPLPPP
QTLPPPPPPS SAAAPPGLS
//
