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 P11623

Entry ID Method Resolution Chain Position Source

No variants for P11623

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P11623

No associated diseases with P11623

2 regional properties for P11623

Type Name Position InterPro Accession
domain Peptidase S39B, luteovirus 207 - 407 IPR000382
domain RNA-directed RNA polymerase, catalytic domain 859 - 974 IPR007094

Functions

Description
EC Number 2.7.7.48 Nucleotidyltransferases
Subcellular Localization
  • [Protein P1-P2]: Membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

5 GO annotations of molecular function

Name Definition
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA-directed 5'-3' RNA polymerase activity Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); uses an RNA template, i.e. the catalysis of RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
serine-type exopeptidase activity Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

3 GO annotations of biological process

Name Definition
DNA-templated transcription The synthesis of an RNA transcript from a DNA template.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
viral RNA genome replication The replication of a viral RNA genome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNRFTAYAAL FFIFSLCSTA KEAGFQHPAF NFRGTSTMSA LSGDYSAAPT PLYKSWALPS
70 80 90 100 110 120
SLNLTTQPPP LLTDRSYYEL VQALISKMRL DCQTVGDMTW RHLSEMLFAS WNSVKEVSLK
130 140 150 160 170 180
AASVTLWAII SIWFGLYWTL ARLITLFLWT FSIEALCLIL LGCITSLIYK GALSLSEHLP
190 200 210 220 230 240
VFLFMSPLKI IWRAAFSKRN YKNEKAVEGY KGFSVPQKPP KSAVIELQHE NGSHLGYANC
250 260 270 280 290 300
IRLYSGENAL VTAEHCLEGA FATSLKTGNR IPMSTFFPIF KSARNDISIL VGPPNWEGLL
310 320 330 340 350 360
SVKGAHFITA DKIGKGPASF YTLEKGEWMC HSATIDGAHH QFVSVLCNTG PGYSGTGFWS
370 380 390 400 410 420
SKNLLGVLKG FPLEEECNYN VMSVIPSIPG ITSPNYVFES TAVKGRVFSD ETVKELEREA
430 440 450 460 470 480
SEAVKKLARF KSLTGKNWAN DYDSDEDYGL EKEAATNAPA EKTAQTNSAE KTAPSTSAEK
490 500 510 520 530 540
TAPTNKPFKW ASGTARQNKR QLRHPRRRYK RTTNGQNGRT DHHSYGGENQ SLGDRGEDSE
550 560 570 580 590 600
QGVSESPAEA QTKQTRKTWR EEQAKQFTSY FDAIYKWGAQ EEGCPPGFRK CGNIPGYYHP
610 620 630 640 650 660
RTKGETKWGQ KLCQVHPELA DKTAGFGWPK AGFEAELQSL NLQAARWLQR AESATIPGAE
670 680 690 700 710 720
ARKRVIEKTV EAYRNCITNA PLCSLKSKLD WAGFQQDIRE AVQSLELDAG VGIPYIAYGL
730 740 750 760 770 780
PTHRGWVEDH KLLPVLTQLT FDRLQKMSEA SFEDMSAEEL VQEGLCDPIR LFVKGEPHKQ
790 800 810 820 830 840
SKLDEGRYRL IMSVSLVDQL VARVLFQNQN KREISLWRSV PSKPGFGLST DTQTAEFLEC
850 860 870 880 890 900
LQKVSGAPSV EELCANHKEH TRPTDCSGFD WSVAYWMLED DMEVRNRLTF NNTQLTERLR
910 920 930 940 950 960
AAWLKCIGNS VLCLSDGTLL AQTVPGVQKS GSYNTSSSNS RIRVMAAYHC GADWAMAMGD
970 980 990 1000 1010 1020
DALEAPNSDL EEYKTLGFKV EVGRELEFCS HIFRNPTLAV PVNTNKMLYK LIHGYNPECG
1030 1040 1050 1060
NPEVIQNYLA AVFSVLQELR HDRELVAKLH QWLVPSATTK EH