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 A2QLK4

Entry ID Method Resolution Chain Position Source
AF-A2QLK4-F1 Predicted AlphaFoldDB

No variants for A2QLK4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2QLK4

No associated diseases with A2QLK4

1 regional properties for A2QLK4

Type Name Position InterPro Accession
domain 1,3-beta-glucan synthase component FKS1-like, domain-1 331 - 443 IPR026899

Functions

Description
EC Number 2.4.1.34 Hexosyltransferases
Subcellular Localization
  • Mitochondrion
  • Cell membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
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.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

1 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).

3 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.
cell wall organization A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
regulation of cell shape Any process that modulates the surface configuration of a cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSGYPAGHYE DGYGHQEHGG DAYYQDEHGQ AYYDPNDYGD SYYDRGNYYN AEGGQAYGQE
70 80 90 100 110 120
GGYYDAGHQD DYYGDQYYDQ GNGAPRGRRR GDSEEDSETF SDFTMRSETA RAADMDYYGR
130 140 150 160 170 180
GDERYNSYAD SQYAGRGYNG YRPPSSQVSY GANRSSGAST PVYGMDYGSA LPGGPRSREP
190 200 210 220 230 240
YPAWASDGQV PVSKEEIEDI FIDLVNKFGF QRDSMRNMYD HLMTQLDSRA SRMTPNQALL
250 260 270 280 290 300
SLHADYIGGD NANYRRWYFA AHLDLDDAVG FANMKLGKAD RKTRKARKAA KAAAQQNPEN
310 320 330 340 350 360
VEENLEAMEG DNSLEAAVYR WKSRMNRMSP HDRVRQLALY MLCWGEANQV RYMPECICFI
370 380 390 400 410 420
FKCADDYYSS PECQSRVEPV EEFTYLNEII TPLYQFCRDQ GYEILDGKYV RRERDHEKII
430 440 450 460 470 480
GYDDMNQLFW YPEGIERISF EDKTRLVDVP PAERWTKLKD VDWKKAFFKT YRETRSWFHM
490 500 510 520 530 540
ITNFNRIWVI HLGAFWFFTA YNAPTLYTKN YQQQLDNKPA GSKYWSAVGF GGALVGLIQI
550 560 570 580 590 600
LATLCEWMYV PRRWAGAQHL SKRLMFLIAV FIVNLAPGVV VFGFNNVLSE TICLIIGIVH
610 620 630 640 650 660
FFIALATFFF FSVMPLGGLF GSYLKKHGRQ YVASQTFTAS YPRLNGNDMW MSYGLWICVF
670 680 690 700 710 720
GAKLVESYFF LTLSLKDPMR ILSPMRIHQC AGVTYIPNSL CHAQPQILLG LMMFMDLTLF
730 740 750 760 770 780
FLDSYLWYVI CNTIFSVARS FYLGVSIWSP WRNIFSRLPK RIYSKVLATT DMEIKYKPKV
790 800 810 820 830 840
LISQVWNAII ISMYREHLLA IDHVQKLLYH QVPSEQEGKR TLRAPTFFVS QEDQSFKTEF
850 860 870 880 890 900
FPAGSEAERR ISFFAQSVAT PMPEPLPVDN MPTFTVLIPH YGEKILLSLR EIIREDEPYS
910 920 930 940 950 960
RVTLLEYLKQ LHPHEWDCFV KDTKILADET SQLNGEPEKN EKDAQKSKID DLPFYCIGFK
970 980 990 1000 1010 1020
SAAPEYTLRT RIWSSLRSQT LYRTISGFMN YSRAIKLLYR VENPEVVQMF GGNSEKLERE
1030 1040 1050 1060 1070 1080
LERMARRKFK ICVSMQRYAK FNKEERENTE FLLRAYPDLQ IAYLDEEPPA NEGEEPRLYS
1090 1100 1110 1120 1130 1140
ALIDGHCELL DNGMRKPKFR IQLSGNPILG DGKSDNQNHS IIFYRGEYIQ VIDANQDNYL
1150 1160 1170 1180 1190 1200
EECLKIRSVL AEFEELTTDN VSPYTPGIAT EAETPVAILG AREYIFSENV GVLGDVAASK
1210 1220 1230 1240 1250 1260
EQTFGTLFAR TLAQIGGKLH YGHPDFLNGI FMTTRGGISK AQKGLHLNED IYAGMTALCR
1270 1280 1290 1300 1310 1320
GGRIKHCEYF QCGKGRDLGF GSILNFTTKI GTGMGEQMLS REYYYLGTQL PLDRFLSFYY
1330 1340 1350 1360 1370 1380
AHPGFHLNNM FIMLSVQMFM IVLINLGALK HETITCRYNS NLPITDPLRP TYCADLTPII
1390 1400 1410 1420 1430 1440
AWVNRCVVSI FIVFFISFVP LAVQELTERG LWRMATRLAK HFGSFSFMFE VFVCQIYANA
1450 1460 1470 1480 1490 1500
VHQNLSFGGA RYIGTGRGFA TARIPFGVLY SRFAGPSIYA GSRLLLMLLF ATSTVWTPAL
1510 1520 1530 1540 1550 1560
IWFWVSLLAL CISPFLFNPH QFAWHDFFID YRDYIRWLSR GNSRSHASSW IAFCRLSRTR
1570 1580 1590 1600 1610 1620
LTGYKRKLLG VPSEKGSGDV PRAKFTNIFF SEIIAPLVQV AVTLVPYLYI NSRTGISNDN
1630 1640 1650 1660 1670 1680
ERASNAVVRI AIVAFGPIGV NAGVSGMFFG MACCMGPIFG MCCKKFGAVL AAIAHAIAVI
1690 1700 1710 1720 1730 1740
ILLVIFEVMF FLESWSWPRM VLGMISAAAI QRFIYKLIIS LALTREFKHD QSNIAWWTGK
1750 1760 1770 1780 1790 1800
WYNMGWHSLS QPGREFLCKI TELGYFSADF VLGHILLFVM LPALCIPYVD KFHSVILFWL
1810 1820 1830 1840 1850 1860
RPSRQIRPPI YSLKQSKLRK RRVVRFAILY FTMLVLFLIL LIAPLVARDE GISVNLNIMS
1870 1880 1890
LMQPLDTDNN DTISSYTGNG LPVGYSAWTP SAASASA