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Database: UniProt
Entry: A0A445JMG6_GLYSO
LinkDB: A0A445JMG6_GLYSO
Original site: A0A445JMG6_GLYSO 
ID   A0A445JMG6_GLYSO        Unreviewed;      2630 AA.
AC   A0A445JMG6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Callose synthase 7 isoform A {ECO:0000313|EMBL:RZB99643.1};
DE            EC=2.4.1.34 {ECO:0000313|EMBL:RZB99643.1};
DE            EC=2.7.7.7 {ECO:0000313|EMBL:RZB99643.1};
GN   ORFNames=D0Y65_022177 {ECO:0000313|EMBL:RZB99643.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB99643.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZB99643.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB99643.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RZB99643.1}.
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DR   EMBL; QZWG01000008; RZB99643.1; -; Genomic_DNA.
DR   Proteomes; UP000289340; Chromosome 8.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   CDD; cd09272; RNase_HI_RT_Ty1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR025724; GAG-pre-integrase_dom.
DR   InterPro; IPR003440; Glyco_trans_48.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR013103; RVT_2.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR12741:SF16; CALLOSE SYNTHASE 7; 1.
DR   PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR   Pfam; PF13976; gag_pre-integrs; 1.
DR   Pfam; PF02364; Glucan_synthase; 4.
DR   Pfam; PF14223; Retrotran_gag_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF07727; RVT_2; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosyltransferase {ECO:0000313|EMBL:RZB99643.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:RZB99643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW   Transferase {ECO:0000313|EMBL:RZB99643.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   TRANSMEM        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2063..2079
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2194..2216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2251..2269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2276..2297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2365..2387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2442..2459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2471..2491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2512..2532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2538..2556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2576..2596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          872..886
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          1041..1216
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1291..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1301..1336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1337..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2630 AA;  302030 MW;  60ED609A0CA5D408 CRC64;
     MQGLRILLIM LGNFRLNSYI SWLQSSLSAS FLAKARSCLP LDYESLASLI SNKFKLFPFA
     ESVFYTKYDF SSTRYTLFWI MLLISKLAFS YYVEILPLVG PTKLIMGLSI DNYQWHEFFP
     ENGQTHNICV VFAIWAPIIL VYFMDTQIWY AIYATLLGFI VGAFSHLGEI RTVEMLHSRF
     QSVPGAFSLR FWTGKDRKTK QVELAETYER NNISYFSQFW NEFINSMRVE DLISDRDRDF
     LLIPYSSTEV SVIQWPVFLL TSKIPIAVDM AKDYKKKTDD DLYKKIRSDG YMFSAVIECY
     ETLKDIILKL LLDEEDRQAV SSICTKVERC IREETFVKEF KMSGLPSLIE KSEKLLTLLQ
     SDDGKLDSKI ANALQDIVEI VIHDVMINGH FFLQKSQQHH VKRGEQFVNI NTSFTHNKSV
     TRKVIRLHLL LTVKESATNV PQNLEARRRI TFFANSLFMN MPKAPKVRDM LSVSILTPYF
     KEDIQYSDEE INKENEEGIS ILFYLTKIYP DEWSNFHERL KSEEVLEENK EELIRQWASY
     RGQTLYRTVR GMMYYRQAMI LQCFIESAAD IALSEGYSET NKKLLEEAQT MADLKFTYVV
     SCQAYGYQRK SKNARDKNCY INILKLMLTH SSLRVAYIDE IEEKTEDGKS QMVYFSVLIK
     GGKKYDEESS SCDQGNSRFL SEYKDQAAGV LFLVLSLLHC IKNTQEIMSN TIRIEKFKGK
     NNFNLWRIKM HALLKEQRVW APVAFASVKK EVASESKEKL EKVYMTKSIC NKLVLKRRLF
     GLHMKEGTSL KDHLDELSSI LIELRDIDVK IEDEDATMIL LASLPSSYKS FVNSLSVESN
     GSGLVVSNSI KNIKKKVFKG KKKTHVNQKD ICNYCKEPGH WKKDCPMKKG KPSAVITKEG
     STSENEFVLS VADHHQHSEN RHVPELKKNL ISIGIMDGKG FKCNTENGVM KIQKGSTMVM
     KGIKRGNLYI LQGTTCVEDG LVAFASRSNK SIPDLTQLWH MRLGHMSEKG MMILQKQQLL
     GNQKLDELKF CEHHVFGKQH RIKFPKAIHT TKGTLDYIHA DCWGPTRVPS LGGGRYFLSI
     IDDYSRMTWI YITSQKSQAF KCFKEWKTLI EKQTERKVKR LKTDNGLEFC STEFNKFCRD
     EGIARQLTVR NTRQQNGVVE RMNKTLLERT RCLLSSVGLN RSFWEKAINT TCFLINKTPS
     TAIGLKTPIE IWNGKTTNYS NLRVFGCNAY YHVNEGKLVP RSRKGLFMGY GDGVKGYRIW
     SPSERKVLLS RDVIFDESHL LHPKIEVPIA GTQSCHSPQE KDVESTTKDS KKRGHTDTSP
     IPQEGEKLEH SSANEAHQNA EPEPTQFNSG ISQRPKRVSK PPERYGFEDM AAYALHVAEE
     IDSNEPATHV VGCKWIFKRK LGLSEKEGIR NKARLVAKGF GQKEGVDFNE IFSPVVKHTS
     IWILLAIVAN QELELEQLDV KTAFLYGRLE ENILMKQLEG FEVQGKESFI TSLGFKRSLY
     DYCVYHNKVE DGSMIYLLLY VDDMLSVAKN MCDKQNLKIL LSGEFDMKDL GAAKKILGME
     IYRDITQKRL FLSQKDYIQK ILVRFGMTDS KPINTPLSEK EKLSAMIKVQ ALADQDYMSK
     VPYSSVVGSL MYAMVYTRPD LAYVVSMISR FLNQPQKEHW KAVQRIFRYL KGTTDVWLIY
     GSNSDCCLTG YSDADFAADL VKKRSLTGYS YTLGGCLVSW KATLQPSVAL STTEAKYMAL
     TEAAKEGIWL RGLINDLRIN QEYANIYYDS LSAICFAKDQ EIYRIKLPGP PTQIGEGKAE
     NQNHAIIFTR GEALQIRDMN QDNYFEESFK MRNVLEEFRK GHEQQKPTIL GIREHIFTGS
     VSSLAWFVSN QKTSYSTIGQ RTLANPLRSS KLYHRSYPRS IVGPPTFPRP KLIALNMKWL
     QGCDTQPLVL DQATIWIRLG PKKMQDPKEA QYQIRWNETD SGTLSLKEAF LIRNPSGLKL
     SVLNAECASW YLPVVYTKQQ RKPRIIISLT ALLLKSGHPK KAPSIIQVDW TPPICNWIKC
     NTDGAAKGAP GPAGCVGIFR DRSAITLGFL FALLVFFYAK NPVVDNCFLV WRVRFHYGHP
     DIFDRIFHIT RGGISKASKI INLSNDIFAG FNSTLRQGFI THNEYIQVGK GHDTGMNQIS
     LFEAKVACEN GEQTLSRDVY RLGQRFDFYR MMSFYFTTVG FYFSSMVTVL IVYAFLYGRL
     YMVLSGVERE ILQSLNIHQS KALEEAMATQ SVVQLGLLLL LPMVMEIGLE RGFRTAVADF
     IIMQLQLASV FFTFQLGTKA HYYGRTLLHG GSKYRPTGRG LIVFHVKFAD NYRMYSRSHF
     VKGLEILLLL IVYELYGESY RSSHLYLFII ISIWFLATSW LFAPFLFNPS GFDLLKTVDD
     WTDWKRWMGY PDGIGISSDR SWESWWDEQN EHLKYSNLRG KIIEIILAFR FFMYQYGIVY
     HMDITHHNKD LLVFGLSWLI LIIILTVLKI VSIERQRFGT DFQLTIRILK ALLFLAFLSV
     MTVLFVVCGL TISDLFAAII AFMPSGWGII QIAQVCKVCF KGAKLWDSVK ELSRTYEYVM
     GSIIFLPIVI LSWFPYVSEF QTRLLFNQGF CRGLQISMIL AGRKDTYKSD
//
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