ID A0A5A7QMC1_STRAF Unreviewed; 1937 AA.
AC A0A5A7QMC1;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN ORFNames=STAS_23052 {ECO:0000313|EMBL:GER46068.1};
OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER46068.1, ECO:0000313|Proteomes:UP000325081};
RN [1] {ECO:0000313|Proteomes:UP000325081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081};
RX PubMed=31522940; DOI=10.1016/j.cub.2019.07.086;
RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L.,
RA Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P.,
RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S.,
RA Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C.,
RA Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T.,
RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I.,
RA Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D.,
RA Shirasu K.;
RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of
RT Plant Parasitism.";
RL Curr. Biol. 29:3041-3052.e4(2019).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:GER46068.1}.
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DR EMBL; BKCP01007404; GER46068.1; -; Genomic_DNA.
DR OrthoDB; 1880850at2759; -.
DR Proteomes; UP000325081; 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:UniProtKB-SubCell.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR FunFam; 1.25.40.270:FF:000002; callose synthase 3; 1.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR058851; CALS1_helical.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
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; PF25968; CALS1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000325081};
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 483..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 520..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 710..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1509..1528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1549..1567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1579..1602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1669..1693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1747..1765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1777..1796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1808..1832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1838..1859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1880..1900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..433
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1937 AA; 223582 MW; 591230AE4B7F30B1 CRC64;
MSSSRGGPSQ QSTPAQRRIT RTPTVGSLGE SIFDSEVVPS SLVEIAPILR VANEVEPSNP
RVAYLCRFYA FEKAHRLDPT SSGRGVRQFK TALLQRLERE NDPTLMGRVK KSDAREMQSF
YQHYYKKYIQ ALQNAADKAD RAQLTKAYQT ANVLFEVLKA VNQTQAVEVD REVLETHDKV
AEKTEIYVPY NILPLDPDSA NQAIMKYPEI QAAVHALRNT RGLPWPKDYK NKKDEDILDW
LQSMFGFQKD NVANQREHLI LLLANVHIRQ FPKPDQQPKL DERSLDEVMK KLFKNYKKWC
KYLDRKSSLW LPTIQQEVQQ RKLLYMGLYL LIWGEAANIR FMPECLCYIY HHMAFELYGM
LAGNVSPMTG ENVKPAYGGE EEAFLKKVVT PIYEVIAQEA ARSKQGRSKH SEWRNYDDLN
ESVSCFRLGW PMRADADFFC KTVDQLRSER DGEIRPTTHR WVGKANFVEI RSYWHIFRSF
DRMWSFFILC LQAMIIVAWN GSGQPSAIFG SDVFKKVLSI FITAAILKLG QAILDLILNW
QARRSMSFHV KLRYILKVLV AAAWVVILPV TYAYSWKGSP PGFLQTIKTW FGHSSSAPSL
FILAVVIYLS PNLLAAILFL FPFIRRFLES SNYKIVMLMM WWSQPRLYVG RGMHESAFCL
FKYTLFWVLL LITKLAFSFY IEIKPLVGPT RTIMDAHVTS YHWHEFFPQA KNNIGVVVVI
WAPVILVYFM DAQIWYAIFS TLFGGVYGAF RRLGEIRTLG MLRSRFQSLP GAFNACLIPE
EKNETVKKKG LKAIFARKFE VIPSSKEKEA ARFSQLWNKI ITSFREEDLI SNREMDLLLV
PYCANRDLEI IQWPPFRLAS KIPIAVDMAK DSNGKDSELR RRIKSDDYMY SAVCECYASF
RNIVKLLVRG KREKEVIEYI FSEVDKHIAE DDLLAEYKLS ALPSLYNLFV ELVKYLLDNK
LEHRDQVVIL FQDMLEVVTR DIMLEDHISN LLDSIHGGPG QEGNVPFDQQ YQLFASAGAI
KFPIPDSEAW KEKVKRLYLL LTVKESAMDV PSNLEARRRI SFFSNSLFMD MPSAPKVRNM
LSFSVLTPYY TEEVLFSLPE LEVPNEDGVS ILFYLQKIFP DEWNNFLERV KCFSEEELRG
SDELEEQLRL WASYRGQTLT RTVRGMMYYR KALEIQAFLD MAKDDDLMEG YKAIELNEDQ
MRGERSLWTQ CQAVSDMKFT YVVSCQLYGI QKRSGDPRAQ DILRLMTTYP SLRVAYIDEV
EEPNKDKSKK VNDKVYYSTL VKAALPKSNS SEPGQNLDQV IYRIKLPGPA ILGEGKPENQ
NHAIIFTRGE GLQTIDMNQD NYMEEALKMR NLLQEFLKRH DVRHPSILGL REHIFTGSVS
SLAWFMSNQE TSFVTICQRL FANPLKVRFH YGHPDVFDRL FHLTRGGVSK ASKVINLSED
IFAGFNSTLR EGNVTHHEYI QVGKGRDVGL NQISLFEAKI ANGNGEQTLS RDLYRLGHRF
DFFRMLSCYF TTIGFYVSTL YXYGRLYLVL SGIEKTLSSQ PEIRQNKPLE VALASQSFVQ
IGFLMALPMM MEIGLEKGFG SALCEFVLMQ LQLAPVFFTF SLGTKTHYYG RTLLHGGAKY
RATGRGFVVF HAKFAENYRL YSRSHFVKAL ELMILLLVYQ IFGTSYRNTV AYVIIMVSMW
FMVGTWLFAP FLFNPSGFEW GKIVDDWAEW NKWIGNRGGI GVPPEKSWES WWEEEGEHLR
HSGKRGILVE VLLALRFFVY QYGLVYHLHI TRHTRSVYGI SWLVILLILF VMKTISVGRR
KFSANFQLVF RLIKGLIFVT FMSILAILIA FARLSPRDIF ICILAFMPTG WGLLLIAQAC
KPVVERAGFW GSVRTLARGF EIVMGLLLFT PVAFLAWFPF VSEFQTRMLF NQAFSRGLQI
SRILGGHRKD RSSRNKE
//
