ID D8U7U1_VOLCA Unreviewed; 1238 AA.
AC D8U7U1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Volvoxopsin-5, sensory rhodopsin with histidine kinase domain {ECO:0000313|EMBL:EFJ44204.1};
GN Name=vop5 {ECO:0000313|EMBL:EFJ44204.1};
GN ORFNames=VOLCADRAFT_95631 {ECO:0000313|EMBL:EFJ44204.1};
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:EFJ44204.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000256|ARBA:ARBA00008130}.
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DR EMBL; GL378366; EFJ44204.1; -; Genomic_DNA.
DR RefSeq; XP_002954798.1; XM_002954752.1.
DR AlphaFoldDB; D8U7U1; -.
DR SMR; D8U7U1; -.
DR STRING; 3068.D8U7U1; -.
DR GeneID; 9621525; -.
DR KEGG; vcn:VOLCADRAFT_95631; -.
DR eggNOG; KOG0519; Eukaryota.
DR eggNOG; KOG1601; Eukaryota.
DR InParanoid; D8U7U1; -.
DR OrthoDB; 314972at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01021; Bac_rhodopsin; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EFJ44204.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW Transferase {ECO:0000313|EMBL:EFJ44204.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 338..555
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 762..880
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 947..1079
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 557..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1110..1137
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1182..1223
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 813
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1238 AA; 131063 MW; 3766370B87F2B88C CRC64;
MGGGGKASTL PAHLQDRIDA IETNQRDTDA QAFQKAVERR ARVSFSVAIA GFGVLMFLLS
AYLLCTSGIG DPELTAEFHS KTDPNCYTWP MVAFSTAFGL NFITLLFERE SAKFQLALLA
CYINFLAGFN DYLSWRGYSP IVRDSWGQGF QLLRTVMWLL TTPAMVYLLS IISDFSRIKV
YSVMLADVLM ISFGILAFLA FNKYLSILLY LVAWVFFSYV VYSMWTMFHA SIAEARHDSS
RVSLEVLRLF AVGLWFTFPG IWIIVKLGLV DVHTEEWMWC ACDFLGKVMF SSSLLHGNFL
TIEQRRLIAM RIVEEGNRIQ VIQELKDLVE QKERFMSSMS HELRTPLNGI IGLSDALLVG
SCGEINDQAL KTITTIKTSG ARLLNLINDI LDAASMRKGK LTIKHEKVNL KRVVDDVIDL
CQPLAKRGVK LVNDLRENVP FVLGDTGRII QVFHNLIGNS CKFTHNGFIS IAASVKDDEV
EVAVSDTGIG IPEDKFDQIF LAFEQVDMSV TRKYGGTGLG LNLVKQLVEA HGGRISVKSK
EGQGTTFFFT LKIHSSAEHP NEGQPQGTPT EAVAGPAEHS QLAAIRGTAA APGGGGGHGH
GPPRRAPSRR GSFTDKMLGA KKTPSEAGKS SLAPGGQNAG AHGQPGGAAR AAAAAAAAPS
ASPQSGEGHG GPAGGAGGIP GGSDAAAAAT AATGVPGSGA GVVRRVSRET GGPGGGGAPA
AGRSVTAGPQ VSGPMSLNDA AALMKGALKR RSSFREKGDK VRVLSVDDDP VNQLVIQNLL
APVGYEILQA MDGQEALQVL KSEERLPDVI LLDVMMPGMS GYEVCRKLRE MYPLSCIPVI
MISAKSKEEH IVEGLAAGSN DYVEILARIA AHLRFRDTVY QAGEMAGALP GEVLPGRLLL
KGGTGGALDL APFLTGPARF TSLPARIARG IESGTTSTTM QMFDQLTLLQ VGIPNLATLL
ANVPASELLV ALAALFHDLD TLLEQHGCYL LEGLDEQMTI VSGLDNVGDQ VLHALGLARS
LLAAADTTAL GSKKLKLCIS IGIHTGPAQA NAGFLVDIAS VSPEAKDSGS FVSAGVAMPA
IASANGGRPA AAGGADGGGG GGGGGDAAAA AAAAAEIAKL KKDYESLEKQ LEEVSNEAAR
LQPYGCMCRV PLYDLDYTVG CESRGSKPKH SARVGSTQHK SVSELECQLE EAARERGGLE
AALAEMEQRL VATHAALASA NHERPGAQSL LLLVQDYY
//
