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 Q8LSC2

Entry ID Method Resolution Chain Position Source
AF-Q8LSC2-F1 Predicted AlphaFoldDB

No variants for Q8LSC2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8LSC2

No associated diseases with Q8LSC2

3 regional properties for Q8LSC2

Type Name Position InterPro Accession
domain Terpene synthase, N-terminal domain 31 - 205 IPR001906
domain Terpene synthase, metal-binding domain 237 - 501 IPR005630
domain Terpene cyclase-like 1, C-terminal domain 237 - 551 IPR034741

Functions

Description
EC Number 4.2.3.23 Acting on phosphates
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
germacrene-A synthase activity Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
diterpenoid biosynthetic process The chemical reactions and pathways resulting in the formation of diterpenoid compounds, terpenoids with four isoprene units.
farnesyl diphosphate metabolic process The chemical reactions and pathways involving farnesyl diphosphate, an intermediate in carotenoid, sesquiterpene, squalene and sterol biosynthesis, as well as a substrate in protein farnesylation.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAVEANGTF QANTKTTEPV RPLANFPPSV WGDRFLSFSL DTTELEGYAK AMEEPKEEVR
70 80 90 100 110 120
KLIVDPTMDS NKKLSLIYSV HRLGLTYLFL QEIEAQLDKL FKEFNLQDYD EFDLYTTSIN
130 140 150 160 170 180
FQVFRHLGHK LPCDVFNKFK DSSSGTFKES ITNDVKGMLG LYESAQLRLR GEPILDEASA
190 200 210 220 230 240
FTETQLKSVV NTLEGNLAKQ VMQSLRRPFH QGMPMVEARM YFSNYDEECS THESLPKLAK
250 260 270 280 290 300
LHFNYLQLQQ KEELRIVSKW WKDMRFQETT PYIRDRVPEI YLWILGLYFE PRYSLARIIA
310 320 330 340 350 360
TKITLFLVVL DDTYDAYATI EEIRLLTDAI NRWDISAMEQ IPEYIRPFYK ILLDEYAELE
370 380 390 400 410 420
KQLAKEGRAK SVIASKEAFQ DIARGYLEEA EWTNSGYVAS FPEYMKNGLI TSAYNVISKS
430 440 450 460 470 480
ALVGMGEMVG EDALAWYESH PKTLQASELI SRLQDDVMTY QFERERGQSA TGVDSYIKTY
490 500 510 520 530 540
GVTEKEAIDE LNKMIENAWK DINEGCLKPR EVSMDLLAPI LNLARMIDVV YRYDDGFTFP
550
GKTMKEYITL LFVGSSPM