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

0 structures for P19028

Entry ID Method Resolution Chain Position Source

No variants for P19028

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P19028

No associated diseases with P19028

2 regional properties for P19028

Type Name Position InterPro Accession
domain Transcription regulator IclR, N-terminal 23 - 111 IPR005471
domain Transcription regulator IclR, C-terminal 84 - 271 IPR014757

Functions

Description
EC Number 2.7.7.49 Nucleotidyltransferases
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

8 GO annotations of molecular function

Name Definition
aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
dUTP diphosphatase activity Catalysis of the reaction: dUTP + H2O = dUMP + H+ + diphosphate.
exoribonuclease H activity Catalysis of the exonucleolytic cleavage of RNA to 5'-phosphomonoester oligonucleotides in both 5' to 3' and 3' to 5' directions.
magnesium ion binding Binding to a magnesium (Mg) ion.
RNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time.
RNA-DNA hybrid ribonuclease activity Catalysis of the endonucleolytic cleavage of RNA in RNA-DNA hybrids to 5'-phosphomonoesters.
zinc ion binding Binding to a zinc ion (Zn).

8 GO annotations of biological process

Name Definition
DNA integration The process in which a DNA segment is incorporated into another, usually larger, DNA molecule such as a chromosome.
DNA recombination Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
dUMP biosynthetic process The chemical reactions and pathways resulting in the formation of dUMP, deoxyuridine monophosphate (2'-deoxyuridine 5'-phosphate).
dUTP catabolic process The chemical reactions and pathways resulting in the breakdown of dUTP, deoxyuridine (5'-)triphosphate.
establishment of integrated proviral latency A process by which the virus integrates into the host genome and establishes as a stable provirus or prophage.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
viral entry into host cell The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.
viral genome integration into host DNA The insertion into a host genome of viral DNA, usually by the action of an integrase enzyme. Once integrated, the provirus persists in the host cell and serves as a template for the transcription of viral genes and replication of the viral genome, leading to the production of new viruses.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
KKFGKLEGGA SCSPSESSAA NSNAICTSNG GKIIGFINYN KVGTTTSLEK RPEILIFVNG
70 80 90 100 110 120
YPIKFLLDTG ADITILNRRD FQVKNSIENG RQNMIGVGGG KRGTNYINVH LEIRDENYKT
130 140 150 160 170 180
QCIFGNVCVL EDNSLIQPLL GRDNMIKFNI RLVMAQISDK IPIVKVKMKD PNKGPQIKQW
190 200 210 220 230 240
PLSNEKIEAL TEIVERLERE GKVKRADPNN PWNTPVFAIK KKSGKWRMLI DFRELNKLTE
250 260 270 280 290 300
KGAEVQLGLP HPAGLQMKKQ ITVLDIGDAY FTNPLDPDYA PYTAFTLPRK NNAGPGRRFV
310 320 330 340 350 360
WCSLPQGWIL SPLIYQSTLD NIIQPFIRQN PQLDIYQYMD DIYIGSNLSK KEHKEKVEEL
370 380 390 400 410 420
RKLLLWWGFE TPEDKLQEEP PYKWMGYELH PLTWTIQQKQ LEIPEKPTLN ELQKLAGKIN
430 440 450 460 470 480
WASQTIPELS IKSLTNMTRG NQNLNSTREW TEEARLEVQK AKRAIEEQVQ LGYYDPSKEL
490 500 510 520 530 540
YAKLSLVGPH QISYQVYQKC PEKILWYGKM SRQKKKAENT CDIALRACYK IREESIIRIG
550 560 570 580 590 600
KEPRYEIPTS REAWESNLIN SPYLKAPPPE VDYIHAALNI KRALSMIKDP PISGAETWYI
610 620 630 640 650 660
DGGRKLGKAA KAAYWTDTGK WQVMELEGSN QKAEIQALLL ALKAGPEEMN IITDSQYMIN
670 680 690 700 710 720
ILSQQPDKME GIWQEVLEEL EKKTAIFIDW VPGHKGIPGN EEVDKLCQTM MIIEGDGILD
730 740 750 760 770 780
KRTEDAGYDL LAAKEIHLLP GEVKVIPTGV KLMLPKGHWG LIMGKSSIGS KGLDVLGGVI
790 800 810 820 830 840
DEGYRGEIGV IMINLSKKSI TLLEQQKIAQ LIILPHKHEA LEQGKVVMDS ERGEKGYGST
850 860 870 880 890 900
GVFSSWVDRI EEAETNHEKF HSDPQYLRTE FNLPKMVAEE IRRKCPVCRI RGEQVGGQLK
910 920 930 940 950 960
IGPGIWQMDC THFDGKIILV AIHVESGYIW AQIISQETAD CTVKAVLQLL SAHIVTELQT
970 980 990 1000 1010 1020
DNGPNFKNQK MEGVLNYMGV KHKFGIPGNP QSQALVENVN QTLKVWVHKF LPETTSLDNA
1030 1040 1050 1060 1070 1080
LALAVHCLNF KQRGRIGGMA PYELLAQQES LRIQDYFSAI PQKLQAQWIY YKDQKDKKWK
1090 1100 1110 1120
GPMRVEYWGQ GSVLLKDEEK GYFLIPRRHV KRVPEPCALP EGDE