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 Q2SF13

Entry ID Method Resolution Chain Position Source
AF-Q2SF13-F1 Predicted AlphaFoldDB

No variants for Q2SF13

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2SF13

No associated diseases with Q2SF13

5 regional properties for Q2SF13

Type Name Position InterPro Accession
domain Peptidase M41 426 - 612 IPR000642
domain AAA+ ATPase domain 208 - 347 IPR003593
domain ATPase, AAA-type, core 212 - 343 IPR003959
conserved_site ATPase, AAA-type, conserved site 315 - 333 IPR003960
domain AAA ATPase, AAA+ lid domain 367 - 409 IPR041569

Functions

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

2 GO annotations of cellular component

Name Definition
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.

5 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.
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNTDPQPPQ KLPLNWVVWT LAVALMLYYL PAMRDRPEPA IKLPYSEFRM LLREGQISSV
70 80 90 100 110 120
TLRGSELDGK FITPRMFPEQ RRQYSRFLTQ LPDFGNEAIL AELEEQNIPL EVKEGHDASS
130 140 150 160 170 180
SKVILLSYLP WIMFMIILFW LSRRTFRNFS GRGGAFDFDK RLETQFECQK PDTTFDEVAG
190 200 210 220 230 240
QTNAKREVQE LVEYLRDPDR FHRVGALAPR GVLLMGPPGT GKTLLARALA GEAGVNFYPM
250 260 270 280 290 300
SASEFIEVFV GVGASRVRQL FKIAKENSPS IIFIDELDSV GRTRGAGYGG GHDEREQTLN
310 320 330 340 350 360
QILAEMDGFA GHDAVIVLAA TNRPDVLDPA LMRPGRFDRH VTLDLPDQEG RVAILKVHAR
370 380 390 400 410 420
HIPLADDVNL NQVAAGTPGF SGADLKNLIN EAAIQAAREN RDHVHSLDFD IARDKIIMGA
430 440 450 460 470 480
ERTLIIPPDE KHRLAVHESG HTLVAYYLPN TDPLYKVSIV PHGRSLGGTH QLPLQERHTY
490 500 510 520 530 540
PEEYLRDKLA VMLAGRIAER ELLGSVSTGA DDDIHQATGL ARAMVSRWGM SKEVGPVDLR
550 560 570 580 590 600
DSEEHPFLGR EMAQPHHHSE FSAEIIDKAV RELLVAAETT AADLISTHRE KLDRLVALLE
610
RSETLHKAQI DECLQTGAS