A7TJT7

PR
Gene name
SUB2-2 (Kpol_1058p53)
Protein name
ATP-dependent RNA helicase SUB2-2
Names
Species
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus)
KEGG Pathway
vpo:Kpol_1058p53
EC number
3.6.4.13: Acting on ATP; involved in cellular and subcellular movement
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-88 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A7TJT7

Entry ID Method Resolution Chain Position Source
AF-A7TJT7-F1 Predicted AlphaFoldDB

No variants for A7TJT7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7TJT7

No associated diseases with A7TJT7

4 regional properties for A7TJT7

Type Name Position InterPro Accession
domain Helicase, C-terminal 289 - 437 IPR001650
domain DEAD/DEAH box helicase domain 83 - 250 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 77 - 280 IPR014001
domain RNA helicase, DEAD-box type, Q motif 58 - 86 IPR014014

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
spliceosomal complex Any of a series of ribonucleoprotein complexes that contain snRNA(s) and small nuclear ribonucleoproteins (snRNPs), and are formed sequentially during the spliceosomal splicing of one or more substrate RNAs, and which also contain the RNA substrate(s) from the initial target RNAs of splicing, the splicing intermediate RNA(s), to the final RNA products. During cis-splicing, the initial target RNA is a single, contiguous RNA transcript, whether mRNA, snoRNA, etc., and the released products are a spliced RNA and an excised intron, generally as a lariat structure. During trans-splicing, there are two initial substrate RNAs, the spliced leader RNA and a pre-mRNA.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

3 GO annotations of biological process

Name Definition
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
mRNA transport The directed movement of mRNA, messenger ribonucleic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
RNA splicing The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSHEGEEDLL EYSDNEQEIQ VDATNINESA VDATVSETAE GATTDSEKKG SYVGIHSTGF
70 80 90 100 110 120
KDFLLKPELA RAIIDCGFEH PSEVQQHTIP QSIHGTDVLC QAKSGLGKTA VFVLSTLQQL
130 140 150 160 170 180
DPVPGEVSVV VICNARELAY QIRNEYLRFS KYMPDVKTAV FYGGTPITKD AELLKNKETA
190 200 210 220 230 240
PHIVVATPGR LKALVRDKLI DLSHVKNFVI DECDKVLEEL DMRRDVQDIF RATPRDKQVM
250 260 270 280 290 300
MFSATLSEEI RPICRRFLQN PLEIFVDDEA KLTLHGLQQY YIKLQENEKN RKLAQLLDDL
310 320 330 340 350 360
EFNQVIIFVK STKRANELTK LLNESNFPAI TVHGNMKQAE RIARYKAFKE FEKRICVSTD
370 380 390 400 410 420
VFGRGIDIER INLAINYDLT TEADQYLHRV GRAGRFGTKG LAISFVSSPE DEEVLGKIQE
430 440
RFDVKIAEFP EEGIDPSTYL NN