B2JID1

PR
Gene name
ligA
Protein name
DNA ligase
Names
Polydeoxyribonucleotide synthase [NAD(+)]
Species
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815) (Burkholderia phymatum)
KEGG Pathway
bph:Bphy_1343
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)

23-102 (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 B2JID1

Entry ID Method Resolution Chain Position Source
AF-B2JID1-F1 Predicted AlphaFoldDB

No variants for B2JID1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2JID1

No associated diseases with B2JID1

12 regional properties for B2JID1

Type Name Position InterPro Accession
domain BRCT domain 602 - 683 IPR001357
domain Helix-hairpin-helix DNA-binding motif, class 1 455 - 474 IPR003583-1
domain Helix-hairpin-helix DNA-binding motif, class 1 489 - 508 IPR003583-2
domain Helix-hairpin-helix DNA-binding motif, class 1 521 - 540 IPR003583-3
domain Helix-hairpin-helix DNA-binding motif, class 1 553 - 572 IPR003583-4
domain Zinc-finger, NAD-dependent DNA ligase C4-type 416 - 443 IPR004149
domain NAD-dependent DNA ligase, OB-fold 331 - 406 IPR004150
domain NAD-dependent DNA ligase, adenylation 16 - 327 IPR013839
domain NAD-dependent DNA ligase, N-terminal 13 - 457 IPR013840
active_site NAD-dependent DNA ligase, active site 124 - 153 IPR018239
conserved_site NAD-dependent DNA ligase, conserved site 340 - 355 IPR033136
domain DisA/LigA, helix-hairpin-helix motif 519 - 582 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
MARTQVPDPA TSAPAERALW LRDELERANY AYYVLDQPDL PDAEYDRLFK ELQQIESEHP
70 80 90 100 110 120
DLITPDSPTQ RVGGEVASGF RPVVHDMPML SLNNGFSDED IAAFDKRVSD TLHHTPVDYA
130 140 150 160 170 180
CELKFDGLAI SLRYVDGQFT QAATRGDGAT GEDVTENVRT IRSIPLKLKG KRVPKLVDVR
190 200 210 220 230 240
GEVLMFRRDF DKLNQRQRDA GQREFANPRN AAAGSLRQLD PKMTAQRPLS FFAYGIGVLD
250 260 270 280 290 300
GIEMPGTHSE LLDWYHEMGL PVNSERAVVQ GAEGVLGFFH KVGEKRDKLP YDIDGVVYKV
310 320 330 340 350 360
NRRDEQDALG FVSRAPRFAL AHKFPAQEAL TKLIAIDVQV GRTGAITPVA RLEPVFVGGA
370 380 390 400 410 420
TVTNATLHNE DEVRRKDIRI GDTVIVRRAG DVIPEVVGAL LERRPPDARE FVMPTQCPVC
430 440 450 460 470 480
GSAIERLPDE AIARCSGGLF CPAQRKQALW HFAQRRALDI DGLGEKIIDQ LVELNLVRTP
490 500 510 520 530 540
ADLFNLGFAT LAELDRFAEK SAQNLIDSLE KAKHTTLARF IYALGIRHVG ESTAKDLARH
550 560 570 580 590 600
FGSLDPIMSA TVEELLEVND VGPIVAEAIH QFFAEEHNRT VIEQLRAPGK VTWAEGPPAP
610 620 630 640 650 660
KAPQGVLAGK TVVLTGTLPN MGRDEAKELL EAAGAKVAGS VSKKTDYVVA GAEAGSKLAK
670 680
AEELGIPVLD EDGMRKLLEG QTT