Q6MRL9

PR
Gene name
ligA
Protein name
DNA ligase
Names
Polydeoxyribonucleotide synthase [NAD(+)]
Species
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
KEGG Pathway
bba:Bd0057
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)

1-109 (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 Q6MRL9

Entry ID Method Resolution Chain Position Source
AF-Q6MRL9-F1 Predicted AlphaFoldDB

No variants for Q6MRL9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6MRL9

No associated diseases with Q6MRL9

11 regional properties for Q6MRL9

Type Name Position InterPro Accession
domain BRCT domain 609 - 684 IPR001357
domain Helix-hairpin-helix DNA-binding motif, class 1 466 - 485 IPR003583-1
domain Helix-hairpin-helix DNA-binding motif, class 1 500 - 519 IPR003583-2
domain Helix-hairpin-helix DNA-binding motif, class 1 564 - 583 IPR003583-3
domain Zinc-finger, NAD-dependent DNA ligase C4-type 428 - 454 IPR004149
domain NAD-dependent DNA ligase, OB-fold 341 - 416 IPR004150
domain NAD-dependent DNA ligase, adenylation 20 - 338 IPR013839
domain NAD-dependent DNA ligase, N-terminal 19 - 468 IPR013840
active_site NAD-dependent DNA ligase, active site 131 - 160 IPR018239
conserved_site NAD-dependent DNA ligase, conserved site 351 - 366 IPR033136
domain DisA/LigA, helix-hairpin-helix motif 530 - 588 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
MPDAFCRDWT SEMGANYSMS KKRHEELKKI ISEHDHNYHV LDKPTITDYE YDQLFAELLD
70 80 90 100 110 120
IEKNPKGLDL SDSPSQRVGG TVLEGFTKAQ HRLPMLSLAN SYSPEDIFEF DERVRKFLNT
130 140 150 160 170 180
EDPVEYLCEL KFDGLSMELI YENGQLVRAI TRGDGTVGED VTHNIKTIKS IPLKLSHKNP
190 200 210 220 230 240
PPLLEVRGEV LMFKEDFARL NETQQENGQQ TFANPRNAAA GTVRQLDSRI AASRPLRFFG
250 260 270 280 290 300
YALGAVEGET FNTQKNIQEY FNDHGIPTVL PYKEDLLVVA KGPEEVVKYY HHIEKVRPKL
310 320 330 340 350 360
PFDIDGVVIK VNSLRLQEDL GLVARSPRWA TAAKFKPEQA QTTVEDIVVQ VGRTGALTPV
370 380 390 400 410 420
AIMKPVKVGG VTVTNATLHN QDEITRKDIR IGDTVIIQRA GDVIPEVVEV VNPDKRPADR
430 440 450 460 470 480
LPYSIPERCP ACDSVAVKAE GEVVTRCVNP LCIAVVKESL KHFVARRAMN IDKVGDRLIE
490 500 510 520 530 540
TLVDNKLLTR FSDFYRLTKE QILSLERQGD KSADNIIKSI ENSKNPTLAR FIFALGIRFV
550 560 570 580 590 600
GEQTGKHLAD HFLTIDKFLE ASEEELLQVP EIGAKVAKSI RDWTGNPKLV DEVKAMIELG
610 620 630 640 650 660
VKIAGPVRAQ EGSLSGMSFL ITGTLPVKRD DAKDLIERNG GKILGSVSSK LNYLVVGDDP
670 680
GSKVEKAQGL GVKIISWEEL QAMI