Q7MBH2

PR
Gene name
ligA
Protein name
DNA ligase
Names
Polydeoxyribonucleotide synthase [NAD(+)]
Species
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
KEGG Pathway
plu:plu1398
EC number
6.5.1.2: Forming phosphoric ester bonds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

20-93 (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 Q7MBH2

Entry ID Method Resolution Chain Position Source
AF-Q7MBH2-F1 Predicted AlphaFoldDB

No variants for Q7MBH2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7MBH2

No associated diseases with Q7MBH2

12 regional properties for Q7MBH2

Type Name Position InterPro Accession
domain BRCT domain 594 - 672 IPR001357
domain Helix-hairpin-helix DNA-binding motif, class 1 446 - 465 IPR003583-1
domain Helix-hairpin-helix DNA-binding motif, class 1 480 - 499 IPR003583-2
domain Helix-hairpin-helix DNA-binding motif, class 1 512 - 531 IPR003583-3
domain Helix-hairpin-helix DNA-binding motif, class 1 544 - 563 IPR003583-4
domain Zinc-finger, NAD-dependent DNA ligase C4-type 407 - 434 IPR004149
domain NAD-dependent DNA ligase, OB-fold 322 - 398 IPR004150
domain NAD-dependent DNA ligase, adenylation 4 - 318 IPR013839
domain NAD-dependent DNA ligase, N-terminal 3 - 448 IPR013840
active_site NAD-dependent DNA ligase, active site 115 - 144 IPR018239
conserved_site NAD-dependent DNA ligase, conserved site 331 - 346 IPR033136
domain DisA/LigA, helix-hairpin-helix motif 510 - 573 IPR041663

Functions

Description
EC Number 6.5.1.2 Forming phosphoric ester bonds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA ligase (NAD+) activity Catalysis of the reaction: NAD+ + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + nicotinamide nucleotide + deoxyribonucleotide(n+m).
metal ion binding Binding to a metal ion.

2 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.
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKSTAQQIEK LRTTLRHHEY LYHVMDAPEI PDAEYDRLMQ ELQDLEEQYP ELITSDSPTQ
70 80 90 100 110 120
RIGAAPLAAF EQVRHEIPML SLDNVFDEES YLAFDKRVRD RLKETQDLVV CCELKLDGLA
130 140 150 160 170 180
VSLLYENGEL VRAATRGDGT TGENITSNIR TIGAIPLRLF GENIPARIEI RGEVFMPQKG
190 200 210 220 230 240
FEKLNEEARR TGAKVFANPR NAAAGSLRQL DPRITAKRPL AFFCYGVGIL EGGELPASHY
250 260 270 280 290 300
ERLIQFKKWG LPVSDKVKVC TDSQQVIDFY HDIVNQRSAL GFDIDGVVVK INSLELQEIL
310 320 330 340 350 360
GFVARAPRWA TAFKFPAQEQ MTIVRDVEFQ VGRTGAITPV ARLEPVQVSG VIVSNATLHN
370 380 390 400 410 420
ADEIERLGLR IGDTVIIRRA GDVIPQVVGV LEERRPQDSN VVVFPEHCPV CGADIERIEG
430 440 450 460 470 480
EAVARCTGGL VCGAQRKEAL RHFVSRRAMD VDGMGEKIID QLVDKEYVKT PADLFRLTAG
490 500 510 520 530 540
KLTGLDRMGP KSAQNVVDAL EKAKKTTFAR FLYALGIREV GEATAANLAA HFGELDKLRS
550 560 570 580 590 600
ADEEALKEVQ DVGEVVAKHV VNFFIEPHNQ TVIDDLIDDI GINWEPVVVT RAEKIDSPFS
610 620 630 640 650 660
GKTVVLTGSL HQLSRDEAKA KLVALGAKVT GSVSKKTDLV IAGEAAGSKL AKANELNIPV
670
IDEEEMIRLL GE