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 Q47281

Entry ID Method Resolution Chain Position Source
AF-Q47281-F1 Predicted AlphaFoldDB

No variants for Q47281

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q47281

No associated diseases with Q47281

5 regional properties for Q47281

Type Name Position InterPro Accession
domain Helicase, C-terminal 410 - 525 IPR001650
domain Helicase/UvrB, N-terminal 167 - 324 IPR006935
domain EcoEI R protein C-terminal domain 649 - 806 IPR013670
domain Helicase superfamily 1/2, ATP-binding domain 164 - 359 IPR014001
domain Type I restriction enzyme R protein, N-terminal domain 33 - 122 IPR029464

Functions

Description
EC Number 3.1.21.3 Endodeoxyribonucleases producing 5'-phosphomonoesters
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
type I site-specific deoxyribonuclease activity Catalysis of the endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5' or 3' protrusions, driven by ATP hydrolysis. Cleavage is dependent on the presence in the DNA of a specific recognition site. Cleavage may occur hundreds or thousands of base pairs away from the recognition site due to translocation of DNA.

1 GO annotations of biological process

Name Definition
DNA restriction-modification system A defense process found in many bacteria and archaea that protects the organism from invading foreign DNA by cleaving it with a restriction endonuclease. The organism's own DNA is protected by methylation of a specific nucleotide, which occurs immediately following replication, in the same target site as the restriction enzyme.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAGVNKTHLT ETDIITKFIL PAVKDAGWDV MSQIRQEVKL RDGKIVVRGK LASRIKVKSA
70 80 90 100 110 120
DIVLYHKPNL PLAVIEAKAN KHAISKGMQQ GLDYASLLDV PFVFASNGDG FIFHDKTNPQ
130 140 150 160 170 180
QLESEIALSD FPTPEQLWQK YCAWKGFTQE QLPVISQDYF DDGSGKAPRY YQMQAINRTV
190 200 210 220 230 240
DAVSAGKNRI LLVMATGTGK TYTAFQIIWR LWKAKNKKRI LFLADRNILV DQTKRNDFQP
250 260 270 280 290 300
FGNAMTKVTG RTIDPAYEVH LALYQAITGP EEHQKAYKQV APDFFDLIVI DECHRGSASE
310 320 330 340 350 360
DSAWREILEY FGSATQVGLT ATPKETEDVS NIDYFGEPVY TYSLKEGIED GFLAPYKVVR
370 380 390 400 410 420
VDIDVDVQGW RPVKGQLDKY GEEIEDRIYN LKDFDRTLVI DERTMLVAQT ITDYLKRTNP
430 440 450 460 470 480
MDKTIVFCND IDHADRMRHA LVVLNPEQVL KNEKYVMKIT GDDDIGKAQL DNFINPKKAY
490 500 510 520 530 540
PVIATTSELM TTGVDAQTCK LVVLDQNIQS MTKFKQIIGR GTRINEKHGK LWFTILDFKK
550 560 570 580 590 600
ATELFADPRF DGLPEKVLVV KPGDISDKDS DFNEQLDAEN NADGGDNDAS EAREDVADYQ
610 620 630 640 650 660
VNRDKQAGNG EFHDDDENKV RKFYVNGVDV KVLAKRVQYY DSDGKLVTES FQDYTRKTML
670 680 690 700 710 720
KDSEYASLDS FVRKWQDAPR KQVIIEELEQ LGILWDVLAE EVGKDLDPFD LLCHVVYGQP
730 740 750 760 770 780
PLTRQERVAN VRKRNYFTKY AEPAQQVLNT LLDKYADEGV QEIEDVQVLK LKPFDTLGRP
790 800 810
IEIIKTRFGD KKAYEQAVNE LENEIYQLPP RSA