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 B2SVK3

Entry ID Method Resolution Chain Position Source
AF-B2SVK3-F1 Predicted AlphaFoldDB

No variants for B2SVK3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2SVK3

No associated diseases with B2SVK3

6 regional properties for B2SVK3

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 403 - 572 IPR000795
domain Small GTP-binding protein domain 405 - 562 IPR005225
domain Translation initiation factor IF-2, N-terminal 327 - 377 IPR006847
domain Initiation factor 2 associated domain, bacterial 70 - 105 IPR013575
domain Translation initiation factor IF- 2, domain 3 680 - 794 IPR023115
domain Translation initiation factor IF-2, domain II 578 - 672 IPR044145

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQQTTIRKL AELVNTPVDK LLVQLAEAGM KFSGPDQVVT STEKMKLLGF LRRTHGKAET
70 80 90 100 110 120
PAEAASEAAK KITLNRRKLQ EVTVSAGRTK TTVNVEVRQK RTYVKSENEG SGRATPMTPD
130 140 150 160 170 180
EERADILAKL AASRQRNLDE QQRLAESDRV RDEEIQRKRD EEQAAKDRAE AERKAAEEAA
190 200 210 220 230 240
AAASAPAPVA AAPTPSAAAP AARAPSSPSS APRPSRPGGA SPASRPSTPA RPDDRNNAAK
250 260 270 280 290 300
HKTRGSHVMV AGVEDDDATK RFAGQLHLSA ADRARRSNVR GKPTGRPGSS SSRRGNDNGR
310 320 330 340 350 360
GSNQANSGPH GFERPTAPVV REVAIGETIT VADLAQKLAL KGGDVVKALF KMGVMATITQ
370 380 390 400 410 420
SIDHDTAALV TEELGHKAVR ADNADFEDAL LAHAEDAQGD TTTRPPVVTI MGHVDHGKTS
430 440 450 460 470 480
LLDYIRRTKI ASGEAGGITQ HIGAYHVETD RGVISFLDTP GHAAFTSMRA RGAKITDIVV
490 500 510 520 530 540
LVVAADDGVM PQTKEAVAHA KAAGVPLIVA VNKIDKAGAD PLRVKNELLA ENVVAEDFGG
550 560 570 580 590 600
DTQFIEVSAK VGTGVDTLLD AISLQAEVLE LKAVAEGRAS GTVIESSLDK GRGPVATVLV
610 620 630 640 650 660
QQGALKRGDY LVCGIQYGRV RALFDETGHQ PGSAGPSIPV QVLGLSGVPE AGDDFVVVDD
670 680 690 700 710 720
ERLAKDVAQQ RETKRRESRL VASATNRMED ILAQMGKGEG QQVLNLVIKA DVQGSVEALK
730 740 750 760 770 780
QSLVALSNED IRINVIHSGV GGITESDANS AAASKATIIG FNVRADASAR KIVESNGVDL
790 800 810 820 830 840
RYFSIIYDVI DQVKQVASGL LGVEIREEIM GIAQVRDVFR SSKFGAVAGC MIIEGVVKRS
850 860 870 880 890 900
KPIRVLRDSV VVFEGELESL RRFKENVDEV RNGNECGIGV KAYNDVKAGD QIECFERIEV
ARTL