ID REPA_MSVK Reviewed; 272 AA.
AC P03568;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 27-MAR-2024, entry version 94.
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 Kenya) (MSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus; Maize streak virus.
OX NCBI_TaxID=10822;
OH NCBI_TaxID=4498; Avena sativa (Oat).
OH NCBI_TaxID=217170; Axonopus compressus.
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 (Red Natal grass) (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=240436; Urochloa deflexa.
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6493977; DOI=10.1093/nar/12.19.7359;
RA Howell S.H.;
RT "Physical structure and genetic organisation of the genome of maize streak
RT virus (Kenyan isolate).";
RL Nucleic Acids Res. 12:7359-7375(1984).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01364};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01364};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
CC {ECO:0000255|PROSITE-ProRule:PRU01364};
CC -!- SUBUNIT: Homooligomer. Interacts with host retinoblastoma-related
CC protein 1 (RBR1), and may thereby deregulate the host cell cycle. Part
CC of the C- and V-complexes which are RepA-Rep-DNA complexes involved in
CC the c-sense and v-sense transcription (By 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=P03568-1; Sequence=Displayed;
CC Name=Rep;
CC IsoId=P14988-1; 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 -!- 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; X01089; CAB37355.1; -; Genomic_DNA.
DR PIR; A04171; QQCVPZ.
DR SMR; P03568; -.
DR Proteomes; UP000008869; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:perturbation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1310.20; -; 1.
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.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR PROSITE; PS52020; CRESS_DNA_REP; 1.
PE 3: Inferred from homology;
KW Activator; Alternative splicing; Covalent protein-DNA linkage;
KW DNA replication; 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; Nucleotide-binding;
KW Nucleotidyltransferase; Repressor; Transferase.
FT CHAIN 1..272
FT /note="Replication-associated protein A"
FT /id="PRO_0000222206"
FT DOMAIN 11..114
FT /note="CRESS-DNA virus Rep endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT REGION 175..187
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 198..202
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 221..230
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT REGION 245..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 18..21
FT /note="RCR-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT MOTIF 60..62
FT /note="RCR-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT MOTIF 100..103
FT /note="RCR-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT COMPBIAS 245..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT BINDING 104
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
SQ SEQUENCE 272 AA; 31390 MW; 376D3E63A8C49C2B CRC64;
MASSSSNRQF SHRNANTFLT YPKCPENPEI ACQMIWELVV RWIPKYILCA REAHKDGSLH
LHALLQTEKP VRISDSRFFD INGFHPNIQS AKSVNRVRDY ILKEPLAVFE RGTFIPRKSP
FLGKSDSEVK EKKPSKDEIM RDIISHSTSK EEYLSMIQKE LPFDWSTKLQ YFEYSANKLF
PEIQEEFTNP HPPSSPDLLC NESINDWLQP NIFQVSPEAY MLLQPACYTL DDAISDLQWM
DSVSSHQMKD QESRASTSSA QQEQENLLGP EA
//
