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REPA_MSVS
ID   REPA_MSVS               Reviewed;         272 AA.
AC   P14990;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Replication-associated protein A;
DE            Short=RepA;
DE            EC=3.1.21.-;
GN   ORFNames=C1;
OS   Maize streak virus genotype A (isolate South Africa) (MSV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Mastrevirus.
OX   NCBI_TaxID=10824;
OH   NCBI_TaxID=4498; Avena sativa (Oat).
OH   NCBI_TaxID=217170; Axonopus compressus.
OH   NCBI_TaxID=240436; Brachiaria deflexa.
OH   NCBI_TaxID=4543; Cenchrus americanus (Pearl millet) (Pennisetum glaucum).
OH   NCBI_TaxID=281129; Cenchrus polystachios.
OH   NCBI_TaxID=4505; Coix lacryma-jobi (Job's tears).
OH   NCBI_TaxID=270102; Dactyloctenium aegyptium.
OH   NCBI_TaxID=66017; Digitaria.
OH   NCBI_TaxID=90396; Echinochloa colona.
OH   NCBI_TaxID=4511; Eleusine coracana (Indian finger millet) (Ragi).
OH   NCBI_TaxID=29674; Eleusine indica (Goosegrass) (Cynosurus indicus).
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH   NCBI_TaxID=59788; Megathyrsus maximus.
OH   NCBI_TaxID=29709; Melinis repens (Natal redtop) (Rhynchelytrum repens).
OH   NCBI_TaxID=4538; Oryza glaberrima (African rice).
OH   NCBI_TaxID=4530; Oryza sativa (Rice).
OH   NCBI_TaxID=158143; Paspalum conjugatum (Hilo grass).
OH   NCBI_TaxID=147272; Paspalum notatum (Bahia grass).
OH   NCBI_TaxID=173849; Paspalum scrobiculatum.
OH   NCBI_TaxID=300125; Rottboellia cochinchinensis.
OH   NCBI_TaxID=4547; Saccharum officinarum (Sugarcane).
OH   NCBI_TaxID=192628; Setaria barbata.
OH   NCBI_TaxID=4565; Triticum aestivum (Wheat).
OH   NCBI_TaxID=4577; Zea mays (Maize).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2829117; DOI=10.1093/nar/16.1.229;
RA   Lazarowitz S.G.;
RT   "Infectivity and complete nucleotide sequence of the genome of a South
RT   African isolate of maize streak virus.";
RL   Nucleic Acids Res. 16:229-249(1988).
RN   [2]
RP   INTERACTION WITH ZEA MAYS RBR1, AND MUTAGENESIS OF 201-ASN-LYS-202.
RC   STRAIN=Isolate Kom;
RX   PubMed=15722543; DOI=10.1099/vir.0.80694-0;
RA   Shepherd D.N., Martin D.P., McGivern D.R., Boulton M.I., Thomson J.A.,
RA   Rybicki E.P.;
RT   "A three-nucleotide mutation altering the Maize streak virus Rep pRBR-
RT   interaction motif reduces symptom severity in maize and partially reverts
RT   at high frequency without restoring pRBR-Rep binding.";
RL   J. Gen. Virol. 86:803-813(2005).
CC   -!- FUNCTION: Implicated in enhancement of V-sense gene expression. Acts a
CC       an inhibitor of C-sense gene transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Interacts (via LXCXE domain) with host
CC       retinoblastoma-related protein 1 (RBR1), and may thereby deregulate the
CC       host cell cycle. Part of the C- and V-complexes which are RepA-Rep-DNA
CC       complexes involved in the c-sense and v-sense transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=RepA;
CC         IsoId=P14990-1; Sequence=Displayed;
CC       Name=Rep;
CC         IsoId=P14989-1; Sequence=External;
CC   -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 may
CC       be involved in metal coordination. RCR-3 is required for phosphodiester
CC       bond cleavage for initiation of RCR.
CC   -!- DOMAIN: The LXCXE motif specifically binds to host RBR1.
CC   -!- MISCELLANEOUS: [Isoform RepA]: Produced from the unspliced transcript.
CC   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000305}.
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DR   EMBL; Y00514; CAA68569.1; -; Genomic_DNA.
DR   PIR; S04806; S04806.
DR   SMR; P14990; -.
DR   Proteomes; UP000006541; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
DR   InterPro; IPR001146; Gemini_AL1_MSV.
DR   InterPro; IPR001191; Gemini_AL1_REP.
DR   InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
DR   InterPro; IPR022692; Gemini_AL1_REP_central.
DR   Pfam; PF00799; Gemini_AL1; 1.
DR   Pfam; PF08283; Gemini_AL1_M; 1.
DR   PRINTS; PR00227; GEMCOATAL1.
DR   PRINTS; PR00229; GEMCOATMSVL1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Endonuclease;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW   Host nucleus; Host-virus interaction; Hydrolase; Metal-binding;
KW   Modulation of host cell cycle by virus; Nuclease; Reference proteome;
KW   Repressor.
FT   CHAIN           1..272
FT                   /note="Replication-associated protein A"
FT                   /id="PRO_0000222208"
FT   REGION          175..187
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250"
FT   REGION          245..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           18..22
FT                   /note="RCR-1"
FT   MOTIF           60..65
FT                   /note="RCR-2"
FT   MOTIF           100..103
FT                   /note="RCR-3"
FT   MOTIF           198..202
FT                   /note="LXCXE motif, interaction with host RBR1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        245..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        100
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         60
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         104
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         201..202
FT                   /note="NE->LI: Complete loss of interaction with RBR1."
FT                   /evidence="ECO:0000269|PubMed:15722543"
FT   MUTAGEN         201..202
FT                   /note="NE->LK: Complete loss of interaction with RBR1."
FT                   /evidence="ECO:0000269|PubMed:15722543"
SQ   SEQUENCE   272 AA;  31329 MW;  36311F3ADDCEED3D CRC64;
     MASSSSNRQF SHRNANTFLT YPKCPENPEI ACQMIWELVV RWIPKYILCA REAHKDGSLH
     LHALLQTEKP VRISDSRFFD INGFHPNIQS AKSVNRVRDY ILKEPLAVFE RGTFIPRKSP
     FLGKSDSEVK EKKPSKDEIM RDIISHATSK AEYLSMIQKE LPFDWSTKLQ YFEYSANKLF
     PEIQEEFTNP HPPSSPDLLC NESINDWLQP NIFQVSPEAY MLLQPTCYTL EDAISDLQWM
     DSVSSHQMKD QESRASTSSA QQEPENLLGP EA
 
 
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