Q9P377
Gene name |
bgs3 (SPAC19B12.03) |
Protein name |
1,3-beta-glucan synthase component bgs3 |
Names |
1,3-beta-D-glucan-UDP glucosyltransferase |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC19B12.03 |
EC number |
2.4.1.34: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9P377
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9P377-F1 | Predicted | AlphaFoldDB |
7 variants for Q9P377
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_4884710_T_A | 238 | L>Q | No | Jeffares_SNPs | |
| I_4885171_G_T | 392 | A>S | No | Jeffares_SNPs | |
| I_4886691_G_T | 898 | L>F | No | Jeffares_SNPs | |
| I_4886867_A_G | 957 | D>G | No | Jeffares_SNPs | |
| I_4886882_G_A | 962 | R>K | No | Jeffares_SNPs | |
| I_4888600_G_A | 1535 | V>I | No | Jeffares_SNPs | |
| I_4889351_T_C | 1785 | V>A | No | Jeffares_SNPs |
No associated diseases with Q9P377
1 regional properties for Q9P377
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 1,3-beta-glucan synthase component FKS1-like, domain-1 | 271 - 383 | IPR026899 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.34 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| 1,3-beta-D-glucan synthase complex | A protein complex that catalyzes the transfer of a glucose group from UDP-glucose to a (1->3)-beta-D-glucan chain. |
| cell division site | The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. |
| cell tip | The region at the end of the longest axis of a cylindrical or elongated cell. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| site of polarized growth | Any part of a cell where non-isotropic growth takes place. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 1,3-beta-D-glucan synthase activity | Catalysis of the reaction: UDP-glucose + [(1->3)-beta-D-glucosyl](n) = UDP + [(1->3)-beta-D-glucosyl](n+1). |
| glucosyltransferase activity | Catalysis of the transfer of a glucosyl group to an acceptor molecule, typically another carbohydrate or a lipid. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| (1->3)-beta-D-glucan biosynthetic process | The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds. |
| beta-glucan biosynthetic process | The chemical reactions and pathways resulting in the formation of beta-glucans. |
| fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process | The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in fungal cell walls. |
| fungal-type cell wall biogenesis | A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin. |
| fungal-type cell wall polysaccharide biosynthetic process | The chemical reactions and pathways resulting in the formation of the polysaccharides which make up the fungal-type cell wall. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDYKKGEHSP | SSSIQILSDD | ATINSNYAYG | EQLQSNDQYN | NIQHPAPSFA | NPFIHEQDDS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YSDILEEEPD | EDAYDSPERP | SSTEEFISQD | ESNISAGSSF | MFPYNRGHPL | SKRHDSIMVD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EFGHEYIVEG | DSIASADEAI | DYDALYASWT | AETKAPILAI | DIENIYIELA | MKFGFQWDNM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RNMFDYLMVM | LDSRASRMTP | QEALLTLHAD | YIGGPQSNFK | KWYFACKMDQ | FDLKSGVLSF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ISRDPSTQVP | YKDMSSCEAL | WISRMDELSN | YERIEQLALY | LLCWGEANNV | RFMPECLCFI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YKVAYDYLIS | PSFKEQKNPA | PKDYFLDNCI | TPLYNLMHDQ | QYEIRDQKYV | RKEKDHASII |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GYDDINQMFW | YSKGLKALLL | SDGSRIMDAD | VASRYFLLAD | IQWQRVCYKS | FRESRTWLHF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LHNFSRIWIL | HISVFWYFTV | YNSPTIYTPN | FHYLEGTQPA | RAAKWCAPAL | AGAVASFISF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LALILEAYFV | PRNNPGAQPV | IPRLIFVSIL | IALNIVPAAF | IFGFSNATQQ | HYRSREIVGY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VHFFFSIGCV | AYQSFIPLPF | LLGPRFKFRS | SSRKYLANSY | FTNDIASLPW | GRTLLSAALW |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ITVFIAKFVE | SYYFLTLSVR | DPIRFLQRMK | PYDCYDFMIG | ASLCSHQPKF | LLSLVYLTDL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VLFFLDTYLW | YMLISTMFSI | AYSFYMGSAI | WTPWRVIFSN | LPRRIYFTLL | AYKDLSTEFK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PKIYVGQIWN | SIMISMYREH | LLSLEHLKGL | LYQQVGSEYF | GKQTFQSPKF | FMEAAKGLNK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| WDAFFRRNSE | AERRISFFAQ | SLGGKIPDAV | PVPKMPSFTV | LIPHYGEKIL | LSLREIIREQ |
| 850 | 860 | 870 | 880 | 890 | 900 |
| DPMSRITLLE | YLKQLYPNDW | DNFVQDTKLM | AGDVGVEETK | SDVKSEKGKK | QGTVKEDLPF |
| 910 | 920 | 930 | 940 | 950 | 960 |
| YCIGFKSTAP | EYTLRTRIWA | SLRSQTLYRT | ASGMMNYSRA | LKLLYRVEQP | NLLDDCDGNF |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| ERLEHQLEQM | AYRKFRLCIS | MQRYAKFNRD | EYENAEFLLR | AHPELQIAYL | DQDPSEDGEE |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| PKVYATLING | FCPFENGRRL | PKYRIRLSGN | PILGDGKADN | QNMALPFVRG | EYLQLIDANQ |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| DNYIEECMKI | RNVLSEFEEM | DCATLTPYTK | KGNARHPVAM | LGAREYVFSE | NSGILGDVAA |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| GKEQTFGTLF | SRSLALIGGK | LHYGHPDFLN | TIFMTTRGGV | SKAQKGLHVN | EDIYAGMTAL |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| QRGGRIKHCD | YFQCGKGRDL | GFGTIINFTT | KIGTGMGEQS | LSREYFYLGT | QLPFFRMLSF |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| YYAHAGFHLN | NVFIMISMQL | LMLVFVNLGA | MYHTVEICDY | QAGAAINASL | YPPGCYMLKP |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| VLDWIRRCII | SIFIVFFISF | LPLVVHDLLE | KGVIRAVARL | CKQIFSLSPM | FEVFVTQNYA |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| NSIFTNLTYG | GARYIATGRG | LATTRVPFSV | LYSLYTGSSI | YLGSRLIMML | LFGTMTVWTT |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| HYVYFWVTMF | ALVICPFIYN | PHQFSFVDFF | VDYREFLRWL | SRGNTKGHAH | SWIGFCRLAR |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| TRITGVNRKV | KGSPSNKLTM | DMPRAGLRNV | IFTEVFLPAC | FAFFTICAYT | FMNSQPGLED |
| 1570 | 1580 | 1590 | 1600 | 1610 | 1620 |
| KSRAVNGFIR | IWIMAALPIA | ISTAALLILL | MFSCMLGPLL | RKCSKRYGAV | LAALAHAVSV |
| 1630 | 1640 | 1650 | 1660 | 1670 | 1680 |
| FGLVFTFEAL | WFLEAWSFSK | TVLGCIVIFA | IHRLVFKLVV | VFLLPREVAS | GENNYSWWDG |
| 1690 | 1700 | 1710 | 1720 | 1730 | 1740 |
| HWFGRKGIPY | MPIQFIREFM | CKVVEMNLFA | MDFILSHCIL | FSLTPILCIP | FIDIPHSVLL |
| 1750 | 1760 | 1770 | 1780 | 1790 | 1800 |
| FWLHPSRQIR | PPIYTRKQNQ | LRRRTFYRYS | LLFFALLCTF | VAMIVVPLVL | DQKLSYQFKF |
| 1810 | 1820 | ||||
| ENSVKFFRLM | QPSLGVLPNT | NKNTSE |