P32282

PR
Gene name
NRDA
Protein name
Ribonucleoside-diphosphate reductase subunit alpha
Names
Protein B1, Ribonucleotide reductase
Species
Enterobacteria phage T4 (Bacteriophage T4)
KEGG Pathway
vg:1258795
EC number
1.17.4.1: With a disulfide as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

581-674 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for P32282

Entry ID Method Resolution Chain Position Source

No variants for P32282

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P32282

No associated diseases with P32282

4 regional properties for P32282

Type Name Position InterPro Accession
domain Ribonucleotide reductase large subunit, C-terminal 220 - 727 IPR000788
domain ATP-cone domain 4 - 93 IPR005144
domain Ribonucleotide reductase, class I, alpha subunit, C-terminal 143 - 731 IPR013346
domain Ribonucleotide reductase large subunit, N-terminal 139 - 216 IPR013509

Functions

Description
EC Number 1.17.4.1 With a disulfide as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
ribonucleoside-diphosphate reductase complex An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin.

1 GO annotations of biological process

Name Definition
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
MQLINVIKSS GVSQSFDPQK IIKVLSWAAE GTSVDPYELY ENIKSYLRDG MTTDDIQTIV
70 80 90 100 110 120
IKAAANSISV EEPDYQYVAA RCLMFALRKH VYGQYEPRSF IDHISYCVNA GKYDPELLSK
130 140 150 160 170 180
YSAEEITFLE SKIKHERDME FTYSGAMQLK EKYLVKDKTT GQIYETPQFA FMTIGMALHQ
190 200 210 220 230 240
DEPVDRLKHV IRFYEAVSTR QISLPTPIMA GCRTPTRQFS SCVVIEAGDS LKSINKASAS
250 260 270 280 290 300
IVEYISKRAG IGINVGMIRA EGSKIGMGEV RHTGVIPFWK HFQTAVKSCS QGGIRGGAAT
310 320 330 340 350 360
AYYPIWHLEV ENLLVLKNNK GVEENRIRHM DYGVQLNDLM MERFGKNDYI TLFSPHEMGG
370 380 390 400 410 420
ELYYSYFKDQ DRFRELYEAA EKDPNIRKKR IKARELFELL MTERSGTARI YVQFIDNTNN
430 440 450 460 470 480
YTPFIREKAP IRQSNLCCEI AIPTNDVNSP DAEIGLCTLS AFVLDNFDWQ DQDKINELAE
490 500 510 520 530 540
VQVRALDNLL DYQGYPVPEA EKAKKRRNLG VGVTNYAAWL ASNFASYEDA NDLTHELFER
550 560 570 580 590 600
LQYGLIKASI KLAKEKGPSE YYSDTRWSRG ELPIDWYNKK IDQIAAPKYV CDWSALREDL
610 620 630 640 650 660
KLFGIRNSTL SALMPCESSS QVSNSTNGYE PPRGPVSVKE SKEGSFNQVV PNIEHNIDLY
670 680 690 700 710 720
DYTWKLAKKG NKPYLTQVAI MLKWVCQSAS ANTYYDPQIF PKGKVPMSIM IDDMLYGWYY
730 740 750
GIKNFYYHNT RDGSGTDDYE IETPKADDCA ACKL