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

19 structures for P54784

Entry ID Method Resolution Chain Position Source
1M4Z X-ray 220 A A/B 1-235 PDB
1ZBX X-ray 250 A A 1-219 PDB
1ZHI X-ray 270 A A 1-219 PDB
5V8F EM 390 A A 1-913 PDB
5ZR1 EM 300 A A 1-914 PDB
6OM3 X-ray 330 A K/L/W/X 2-214 PDB
6RQC EM 440 A A 1-914 PDB
6WGC EM 430 A A 1-913 PDB
6WGG EM 810 A A 1-913 PDB
6WGI EM 1000 A A 1-913 PDB
7E9C EM 350 A K 2-219 PDB
7E9F EM 400 A K/L 2-219 PDB
7MCA EM 360 A A 1-914 PDB
7TJF EM 260 A A 1-914 PDB
7TJH EM 250 A A 1-914 PDB
7TJI EM 270 A A 1-914 PDB
7TJJ EM 270 A A 1-914 PDB
7TJK EM 270 A A 1-914 PDB
AF-P54784-F1 Predicted AlphaFoldDB

15 variants for P54784

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-142702 165 V>I No SGRP
s13-142831 208 L>M No SGRP
s13-142984 259 D>N No SGRP
s13-143064 285 E>D No SGRP
s13-143070 287 D>E No SGRP
s13-143134 309 G>R No SGRP
s13-143141 311 K>T No SGRP
s13-143356 383 A>S No SGRP
s13-143587 460 Y>H No SGRP
s13-144203 665 N>S No SGRP
s13-144245 679 K>R No SGRP
s13-144403 732 K>E No SGRP
s13-144479 757 A>V No SGRP
s13-144518 770 V>A No SGRP
s13-144592 795 T>A No SGRP

No associated diseases with P54784

4 regional properties for P54784

Type Name Position InterPro Accession
domain Bromo adjacent homology (BAH) domain 48 - 188 IPR001025
domain AAA+ ATPase domain 471 - 628 IPR003593
domain ATPase, AAA-type, core 475 - 620 IPR003959
domain AAA lid domain 638 - 738 IPR041083

Functions

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

5 GO annotations of cellular component

Name Definition
DNA replication preinitiation complex A protein-DNA complex assembled at eukaryotic DNA replication origins immediately prior to the initiation of DNA replication. The preinitiation complex is formed by the assembly of additional proteins onto an existing prereplicative complex. In budding yeast, the additional proteins might include Cdc45p, Sld2p, Sld3p, Dpb11p, DNA polymerases, and others; in fission yeast the GINS complex is present.
nuclear origin of replication recognition complex A multisubunit complex that is located at the replication origins of a chromosome in the nucleus.
nuclear pre-replicative complex A protein-DNA complex assembled at eukaryotic DNA replication origins during late mitosis and G1, allowing the origin to become competent, or 'licensed', for replication. The complex normally includes the origin recognition complex (ORC), Cdc6, Cdt1 and the MiniChromosome Maintenance (Mcm2-7) proteins.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

6 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.
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
DNA replication origin binding Binding to a DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally.
metal ion binding Binding to a metal ion.
nucleosome binding Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.

5 GO annotations of biological process

Name Definition
DNA replication initiation The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
maintenance of rDNA Any process involved in sustaining the fidelity and copy number of rDNA repeats.
mitotic DNA replication checkpoint signaling A signal transduction process that contributes to a mitotic DNA replication checkpoint.
pre-replicative complex assembly involved in nuclear cell cycle DNA replication The aggregation, arrangement and bonding together of a set of components to form the nuclear pre-replicative complex, a protein-DNA complex that forms at the eukaryotic DNA replication origin and is required for replication initiation.
silent mating-type cassette heterochromatin assembly Repression of transcription at silent mating-type loci by alteration of the structure of chromatin.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O16810 Orc1 Origin recognition complex subunit 1 Drosophila melanogaster (Fruit fly) EV
Q13415 ORC1 Origin recognition complex subunit 1 Homo sapiens (Human) PR
Q9Z1N2 Orc1 Origin recognition complex subunit 1 Mus musculus (Mouse) PR
Q80Z32 Orc1 Origin recognition complex subunit 1 Rattus norvegicus (Rat) PR
Q710E8 ORC1A Origin of replication complex subunit 1A Arabidopsis thaliana (Mouse-ear cress) PR
Q9SU24 ORC1B Origin of replication complex subunit 1B Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAKTLKDLQG WEIITTDEQG NIIDGGQKRL RRRGAKTEHY LKRSSDGIKL GRGDSVVMHN
70 80 90 100 110 120
EAAGTYSVYM IQELRLNTLN NVVELWALTY LRWFEVNPLA HYRQFNPDAN ILNRPLNYYN
130 140 150 160 170 180
KLFSETANKN ELYLTAELAE LQLFNFIRVA NVMDGSKWEV LKGNVDPERD FTVRYICEPT
190 200 210 220 230 240
GEKFVDINIE DVKAYIKKVE PREAQEYLKD LTLPSKKKEI KRGPQKKDKA TQTAQISDAE
250 260 270 280 290 300
TRATDITDNE DGNEDESSDY ESPSDIDVSE DMDSGEISAD ELEEEEDEEE DEDEEEKEAR
310 320 330 340 350 360
HTNSPRKRGR KIKLGKDDID ASVQPPPKKR GRKPKDPSKP RQMLLISSCR ANNTPVIRKF
370 380 390 400 410 420
TKKNVARAKK KYTPFSKRFK SIAAIPDLTS LPEFYGNSSE LMASRFENKL KTTQKHQIVE
430 440 450 460 470 480
TIFSKVKKQL NSSYVKEEIL KSANFQDYLP ARENEFASIY LSAYSAIESD SATTIYVAGT
490 500 510 520 530 540
PGVGKTLTVR EVVKELLSSS AQREIPDFLY VEINGLKMVK PTDCYETLWN KVSGERLTWA
550 560 570 580 590 600
ASMESLEFYF KRVPKNKKKT IVVLLDELDA MVTKSQDIMY NFFNWTTYEN AKLIVIAVAN
610 620 630 640 650 660
TMDLPERQLG NKITSRIGFT RIMFTGYTHE ELKNIIDLRL KGLNDSFFYV DTKTGNAILI
670 680 690 700 710 720
DAAGNDTTVK QTLPEDVRKV RLRMSADAIE IASRKVASVS GDARRALKVC KRAAEIAEKH
730 740 750 760 770 780
YMAKHGYGYD GKTVIEDENE EQIYDDEDKD LIESNKAKDD NDDDDDNDGV QTVHITHVMK
790 800 810 820 830 840
ALNETLNSHV ITFMTRLSFT AKLFIYALLN LMKKNGSQEQ ELGDIVDEIK LLIEVNGSNK
850 860 870 880 890 900
FVMEIAKTLF QQGSDNISEQ LRIISWDFVL NQLLDAGILF KQTMKNDRIC CVKLNISVEE
910
AKRAMNEDET LRNL