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 P30620

Entry ID Method Resolution Chain Position Source
AF-P30620-F1 Predicted AlphaFoldDB

10 variants for P30620

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-544896 23 S>G No SGRP
s13-544878 29 K>E No SGRP
s13-544601 121 E>V No SGRP
s13-544578 129 V>I No SGRP
s13-544380 195 A>S No SGRP
s13-543971 331 L>P No SGRP
s13-543761 401 L>S No SGRP
s13-543705 420 F>V No SGRP
s13-543273 564 S>G No SGRP
s13-543223 580 N>K No SGRP

No associated diseases with P30620

2 regional properties for P30620

Type Name Position InterPro Accession
domain Rad18, zinc finger UBZ4-type 144 - 174 IPR006642
domain DNA repair metallo-beta-lactamase 488 - 637 IPR011084

Functions

Description
EC Number
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
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

4 GO annotations of molecular function

Name Definition
5'-3' exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a DNA molecule.
5'-3' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 5' end.
damaged DNA binding Binding to damaged DNA.
metal ion binding Binding to a metal ion.

4 GO annotations of biological process

Name Definition
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
double-strand break repair via nonhomologous end joining The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
interstrand cross-link repair Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA. DNA interstrand crosslinks occur when both strands of duplex DNA are covalently tethered together (e.g. by an exogenous or endogenous agent), thus preventing the strand unwinding necessary for essential DNA functions such as transcription and replication.
protection from non-homologous end joining at telomere A process that prevents non-homologous end joining at telomere, thereby ensuring that telomeres do not fuse.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSRKSIVQIR RSEVKRKRSS TASSTSEGKT LHKNTHTSSK RQRTLTEFNI PTSSNLPVRS
70 80 90 100 110 120
SSYSFSRFSC STSNKNTEPV IINDDDHNSI CLEDTAKVEI TIDTDEEELV SLHDNEVSAI
130 140 150 160 170 180
ENRTEDRIVT ELEEQVNVKV STEVIQCPIC LENLSHLELY ERETHCDTCI GSDPSNMGTP
190 200 210 220 230 240
KKNIRSFISN PSSPAKTKRD IATSKKPTRV KLVLPSFKII KFNNGHEIVV DGFNYKASET
250 260 270 280 290 300
ISQYFLSHFH SDHYIGLKKS WNNPDENPIK KTLYCSKITA ILVNLKFKIP MDEIQILPMN
310 320 330 340 350 360
KRFWITDTIS VVTLDANHCP GAIIMLFQEF LANSYDKPIR QILHTGDFRS NAKMIETIQK
370 380 390 400 410 420
WLAETANETI DQVYLDTTYM TMGYNFPSQH SVCETVADFT LRLIKHGKNK TFGDSQRNLF
430 440 450 460 470 480
HFQRKKTLTT HRYRVLFLVG TYTIGKEKLA IKICEFLKTK LFVMPNSVKF SMMLTVLQNN
490 500 510 520 530 540
ENQNDMWDES LLTSNLHESS VHLVPIRVLK SQETIEAYLK SLKELETDYV KDIEDVVGFI
550 560 570 580 590 600
PTGWSHNFGL KYQKKNDDDE NEMSGNTEYC LELMKNDRDN DDENGFEISS ILRQYKKYNK
610 620 630 640 650 660
FQVFNVPYSE HSSFNDLVKF GCKLKCSEVI PTVNLNNLWK VRYMTNWFQC WENVRKTRAA
K