ID A0A9P1DJH1_9DINO Unreviewed; 3169 AA.
AC A0A9P1DJH1;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=C1SCF055_LOCUS35115 {ECO:0000313|EMBL:CAI4009783.1};
OS Cladocopium goreaui.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Cladocopium.
OX NCBI_TaxID=2562237 {ECO:0000313|EMBL:CAI4009783.1};
RN [1] {ECO:0000313|EMBL:CAI4009783.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen Y., Dougan E. K., Chan C., Rhodes N., Thang M.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAL4797095.1, ECO:0000313|Proteomes:UP001152797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Chen Y., Shah S., Dougan E. K., Thang M., Chan C.;
RL Submitted (MAY-2024) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + UDP + H(+); Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00047777};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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:CAI4009783.1}.
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DR EMBL; CAMXCT010004635; CAI4009783.1; -; Genomic_DNA.
DR EMBL; CAMXCT020004635; CAL1163158.1; -; Genomic_DNA.
DR EMBL; CAMXCT030004635; CAL4797095.1; -; Genomic_DNA.
DR OrthoDB; 421992at2759; -.
DR Proteomes; UP001152797; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.490.10; Globins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR12741:SF48; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP001152797};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1963..1987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2007..2026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2046..2069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2081..2100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2121..2141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2194..2211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2808..2831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2851..2872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2956..2980
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2986..3007
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3089..3114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3126..3147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 501..786
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 79..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..139
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3169 AA; 353257 MW; ED54FE53F134AB69 CRC64;
MQVDGAEDPV AGRLRKEHRK LADLLSTREG QVYFLVKFLV QRGSEVAEEF RHRLKKGQPI
HARGYNFSEE VITEALQQWE GKGTSTARSP VPESSATEHN EGKATGQATG IAATKSREKP
EVPRPTQAEP APQVAQVAAS DLRPSTAVSP EFWHQGWREA RLAKLHERQP EKATFLQEPE
KFLQDLDGDG RSQSTVWGYN SFSAGSGERK VGRLGLHREE DLDLDFSSAL EVDLGRGLGT
SVTRDSFGFS SHHSVGVRRA PGGVDRATSF QAASNRPNQG LEQMPFDHQI RGMRWKGEGV
CCFILAGSGG IDAFRASRVL PHLLHLSTLS SGHLGQADLS GFRACVLLCD LMEWPASQDD
AKDLFSACKE LASNGSAVAV IAVFLAPIPG GPDRDAASTQ ALHSAVLAAG ADCVLFSCPT
HPVTFRHLQA AIQGTEAWHE RIAEAIESAQ AKLARAQEQR WQRHYQIALR KIVWKAPQTV
FPHIPQEDAD LAERDDGVGD YSFVRVIGSG AFGSVFLGRH PRFGDVAIKA IKKASIKNVF
DLAKVERELS ILMGVLDHPN VLEILSCLHG ANNLYIVMQF LGEYTLHTYL QLRQTGSARN
VLMLPFQEVQ GIFGDILKAI AHCHAAHVCH RDLKFKNMMI DANSRVTMVD FGLAVQVAPG
QELHDSCGTV PFAAPEVMTC SSTKGYEGTS ADTWSIAVCL VELLCGLGTV DSIIGLTQDD
ESNFDHIAQQ CLLLCTDYVH QLVLSYAGKD VQGGHRNDLV KTMRGVFREN PKSRMSVRDI
GALEAFSAKA GPLPKAKRLR DPNDDDERSS WTHSQISQGP KSQGSGEEET LSDLSVNEWM
GPEAGDLRQV LPLLERIGGS QTVVKVVSTV YDWLLPRPEF GKFFLACPLK MGRIRAGISS
FLTELLEDST KVDLEMLSNV HWNLGVSDFL FTDFADALLE AFRTWGSRGD SNMAEIQRCL
EKVRLPITAG HRARLAAAQT DRCPQEIVWL NSSLDCSEDD FAQALSDLLL QDARLEACLN
EDMRDQMSSS AVLSFARTFW QGSVDGAMEV VFAGETPLFQ QDIGAVSLFC ENVRQVLAEI
GMEESDARDI QVLMEHSGEL VLNRARNAKL VQSPSMAHDI TWFTKTLTSL CKADPFLQFF
ADNPKMQNCM ESIFGLVMNG GTPPAGPSWN SRLRTAHQDL YLTDARYSAF IAHIDKVLRA
MFPWPVHPAA VANSNIRSLE GFRTEVLCGS TLRSSRLQAV EGMLNSSDSS KQRVARQARK
GRVVSAMQRC AVQLFNAIVL DPRVAVFFKN SDPACKDRKA RYLGCALAGN LPTVSAHAGA
GANPPSTPAS ERSEKSTISP TSSLKQQHQH FRISDYHFDV FLDHVRRALA GEDPEAADLA
PAQLEALRPN VVIDSRAACP VSGATASNGR GCPFRRPMVE GTPLLEKVGG TEEIEKILTL
MEREAGQRFV SVIEAVAMWL WPLWCAFLWH VAGHQGIPQD ELGGIGGDGW VELPKVVDPT
CSCQPSSSAS DGELLQLSQW NCLRIHQAGV DYATLAANYG QNVNQDWKER LQAATAMCDQ
AKKETDLKAA AQSACCAWGD VLMQQRECCN VPGPPYCTNP TDSKLGHASA LVLALLLALL
AAGLPKCGAS FFAPSLMLAK ASAPVEEDEA QEVYRAKAAP QVSELAQELE ATWERSSLRN
LKQAKEWKAH SAHCFAAMQV AFDFQKDSVK NQYEHFISLL RSHVSVVCDR EKRRQPQICE
ETALLAHALK ELHDDILASC LPWQQQFLSV SQEAELGASQ RHQWCSIKDA GARYPAAFRE
LEELVLFLLI WGEAGNLRNM PEMLYFIYHV MLEADSSCHF QAGAVVSALR ASGSLHGSSH
AFLVDIVRPI YRVIFDEHYV AVKVKPDGKD DKKIRPTYDR YLPPDSANYD DWNELFQDIP
RLLGKVAALM RQSRTRRYYF LRQLPWRKIL KDAKTHRELH SWWGVWAGTH RIWFLHSLLF
FLSMFWVSSR SFQSNASGWS VFLGGNSPLV CLSFVGLLVP AHLFLWKLGT WFTTGIALRR
GRALGVILFI LQVLCGCIPV VTFLLVRYLD AVDSPELSAA LWIHAFVCCL GALVILLQPC
ENGDKLRHAT GSSWTAKLLR WLFWVTVLAV KWLVGLGSIA ATQQAITDLR TSQPGREALN
ELPQVAFGPN WDKDMVEWLA IWGTGFICYV ADTQYWFVLG CGLLGFVLSV YQRGWRLYTL
VSEDAICGVP QRFAERVILA APRGNQNFAS QAQGPVPVPS ARRQWWVKWF PDLWDRIVDF
MHCEDKLDDF IIGQMKFGPD ARNRVSMEML CHEPIEAKSR FLPPAIFTHS SCVQRSMRRD
LGILPDETWP WNVEVQWRLN AFARNLASED LPRPFLTPYV PGLTVLIPHY GEQILLRRRD
LEIAVANAGE EVPLIAWLEK RYHGDFTAFT SRMTRLHERW PRAGSRWDQY QDNHWEEICM
WASMRSQTLW RTVEGLMLYQ PALDCFNQMV ERENQRSLLL WDSYEVFTCM VSMQMYAFFD
DDQYRHTEKL LERFQRPDRA GQTPWQSFQI AFIDFKEKGE NANADGIHAA QERRYFSCLI
DPGCAREGLR RKPRLTVELP GFPILGDGKG DNQNHAIIFS RGSIIQCIDA NQGGYFEQML
LLPCALGEFR QEGPGLNPRI VGFAEHITSD IGSLGDFAAG AETAFGTVLQ RCYSFLGGRM
HYGHPDMMNK EFMIQQGGVS KATKTVNLSE DIFAGMDFTL RGNGRNIVHR EYLHVAKGRD
LGFNTILTFF SKLSAGTGEQ LLTRQVLRLG HELDLPEFLT FYYAHAGFYL TQFFLSKSIP
LLVFIWLVVV LDDPEQNFPA MDPDSKGTSG ATVIATMLIT QFSKLLLLFI VAQLAPLFMQ
VWLESSIVSA FLRVIKQIFT LAPLHFVFQA KVIGNYITNE VTLGGAKYLP TGRGLPTTRR
AFLRRLDKGG GLYNDYAVLA LYDGAQLLLA VLLVILGGGL AVQLSLFWWL LALGLTICSW
LLAPFIFNPY QFAHTHFRAD LGDWKEFFFD GKGRYWAEWY TKTRLLPGAG LRSSGVEIIK
RGLFLGAWYT ILNQKVHMLT VIFSGSSRLI FSIGLVAMPP IGMSLVACCI LPALPSLWGQ
PGEPLALGWS ALTVVLLDCL ETILYLWKLI CVKWWKSFAV GLGWMDDVG
//
