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 Q54N97

Entry ID Method Resolution Chain Position Source
AF-Q54N97-F1 Predicted AlphaFoldDB

No variants for Q54N97

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54N97

No associated diseases with Q54N97

4 regional properties for Q54N97

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 6 - 238 IPR003439
domain AAA+ ATPase domain 32 - 215 IPR003593
domain Transport-associated OB, type 2 276 - 344 IPR013611
conserved_site ABC transporter-like, conserved site 138 - 152 IPR017871

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
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
delta DNA polymerase complex A multimeric DNA polymerase enzyme complex which differs in composition amongst species; in humans it is a heterotetramer of four subunits of approximately 125, 50, 68 and 12kDa, while in S. cerevisiae, it has three different subunits which form a heterotrimer, and the active enzyme is a dimer of this heterotrimer. Functions in DNA replication, mismatch repair and excision repair.

6 GO annotations of molecular function

Name Definition
3'-5'-exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule.
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
metal ion binding Binding to a metal ion.
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.

5 GO annotations of biological process

Name Definition
base-excision repair, gap-filling Repair of the damaged strand by the combined action of an apurinic endouclease that degrades a few bases on the damaged strand and a polymerase that synthesizes a 'patch' in the 5' to 3' direction, using the undamaged strand as a template.
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.
DNA replication proofreading Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
nucleotide-excision repair, DNA gap filling Repair of the gap in the DNA helix by DNA polymerase and DNA ligase after the portion of the strand containing the lesion has been removed by pyrimidine-dimer repair enzymes.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKRSIVTGGG NNDKKFKAQP PPKNNYRGGG DDEEDDEFEE DDDEDEGDEF GEEEDEDDID
70 80 90 100 110 120
VENIIASDSM DIDIQDDGSQ QLFLWSRKPV QDLVPHKKPL IFQQLEVDYT EIKEPVPGMP
130 140 150 160 170 180
GPKVGPLPAI RLFGVTKEGN SVLCKVHGFL PYFFISCPPG FTEADCKSLK HDLNESMKMS
190 200 210 220 230 240
SNQSNEKDIE NIVVSIDIEK KKSIMGYNPN PLSDFIRITL ILPKFVTRCR EIFESGRHHF
250 260 270 280 290 300
TIPGQPFRQY QTYESNILFA LRFLIDKGIT GCSWIELPAN TYKLSETPVS TCQIEVDTSL
310 320 330 340 350 360
ETIISLSDDD SPAPYRILSF DIECAGRKGV FPEPEKDPVI QISNIVKNNG DAEPFIKNIF
370 380 390 400 410 420
TLKGCSSIVG AHVIPHKREE DLLREWRKFV IKVDPDVIIG YNIVNFDIPY LISRARQLKI
430 440 450 460 470 480
PEFALLGRIK TTISKIKSTR FSSSNLGTRE SKEISMPGRT QFDLMQAIQR DHKLTSYSLN
490 500 510 520 530 540
NVSAHFLKEQ KEDVHFSIIS DLQNGTDDDR RRLAVYCIKD AVLPMRLLDK LMILINYTEM
550 560 570 580 590 600
ARVTGVPLSY LLGRGEGIKV LSQLYRKAMV ENFLIPTYKV TGKGEKFQGA IVIEPTPGFY
610 620 630 640 650 660
DTPIATLDFT SLYPSIMMAH NLCYSTLLSA EEAKKLPPEI YTTTPFGDHF IKSDTKKGLL
670 680 690 700 710 720
PRILEELLSA RKKAKDELKN EKDPFKRAVL DGRQLALKIS ANSVYGFTGA RVGKLPCLEI
730 740 750 760 770 780
SRSVTSFGRE MLDKTKKIVE ERYTIANGYK HDAVIIYGDT DSVMVKFGVK TVAEAMEMGR
790 800 810 820 830 840
DAAKFVTTTF IRPINLDFEK VYYPYLLMAK KKYAGLYWTK PDIHDRMDVK GLEMVRRDTC
850 860 870 880 890 900
LLVRNVVSTI LKKILIEKDL KSAEEYTKSV ISDLLQNRLD LSMLVITKAL SKTQYKGKVI
910 920 930 940 950 960
HNELARKMRA RDPATAPNLG DRVPYVVIQG SKGAPIYEKA EDPLYALEHN ILLDCQYYLD
970 980 990 1000 1010 1020
KQLKAPLIRI FKPIMSNPDL IFHGEHTRTI AQSTLSDNNK GFFGTLKKKK VCMNCPKELT
1030 1040 1050 1060 1070 1080
DTESTTCINC QHKEASLYQT SLEKVTSLET KFSEAWTQCQ RCSGSLHQPV LCSNRDCPIF
1090 1100
YMRTKVQLDL IEAKKTLNRF NVEW