P19199 (POL_COYMV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Polyprotein P3 Including the following 5 domains: Putative movement protein Short name=MP Capsid protein Alternative name(s): Coat protein Short name=CP Protease Short name=PR EC=3.4.23.- Reverse transcriptase Short name=RT EC=2.7.7.49 Ribonuclease H EC=3.1.26.4
Organism	Commelina yellow mottle virus (CoYMV)
Taxonomic identifier	10653 [NCBI]
Taxonomic lineage	Viruses › Retro-transcribing viruses › Caulimoviridae › Badnavirus
Virus host	Commelina [TaxID: 4743]

Protein attributes

Sequence length	1886 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Capsid protein self assembles to form a bacilliform capsid about 90-900 nm in length. The capsid encapsulates the genomic dsDNA. Following virus entry into host cell, provides nuclear import of the viral genome. Virus particles do not enter the nucleus, but are targetted to the nuclear membrane through the interaction with host importins By similarity.
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Post-translational modification	Polyprotein P3 is presumably proteolytically cleaved into several chains by viral protease Potential.
Sequence similarities	Contains 1 CCHC-type zinc finger. Contains 1 peptidase A11 domain. Contains 1 peptidase A2 domain. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.

Ontologies

Keywords
Biological process	Initiation of viral infection Transport Viral penetration into host nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Aspartyl protease Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase Viral movement protein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW spread of virus in host, cell to cell Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1886	1886	Polyprotein P3		PRO_0000199569
Regions
	Domain	1215 – 1292	78	Peptidase A2
	Domain	1425 – 1615	191	Reverse transcriptase
	Domain	1736 – 1841	106	RNase H
	Zinc finger	879 – 896	18	CCHC-type
	Compositional bias	480 – 486	7	Poly-Lys
Sites
	Active site	1220	1	For protease activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19199 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: 60E010C132FEDA91	FASTA	1,886	215,662
	10 20 30 40 50 60 MATRRLPAVT QTDGSRTATE SGVPEYEDQI RSYRNDQRRR HIWAGRGRRL LSIMPGVSSS 70 80 90 100 110 120 ERTLEMQMNP EVQLQRSMNH RAEAVPAEVL YRTFHGSVNH RVYSHRSEER MMVVNGSQVD 130 140 150 160 170 180 RSFIQESSFE VLSRTGIEFI HIGVMLVRIQ ILHRKFAGTM ALIVFRDTRW SDDRAVLAAM 190 200 210 220 230 240 EIDLSEGNQI VYVLPDIMMT IKSFYRHIQI CVMTKGYDGW QGEDNLLITR GLTGRLSNTS 250 260 270 280 290 300 NVGFAYDVKA MVEHLQSNGV KAIKGEKWDA KRFHNGQWNI EPSKVVVPMQ PTEMKAVSNY 310 320 330 340 350 360 DGTTSLRFSN YAAASTSKPP QYNEKDEEIN EDEQEINHSL NLILNDEEST DEDEEYYQYQ 370 380 390 400 410 420 RYAWSQVGDS TFYYDTDGVW EEIDRCNDLP EYVPSETSTP TIDESEAIID EFLEHAYEQR 430 440 450 460 470 480 CDSDESLQSG DPRKYEYPTP QSSPEHLDNE SRSRSSSASS TSMQDDVEEI VRLMKEMRMK 490 500 510 520 530 540 KQKKKKAQQA LSSQAQEEPI IEENIEENKQ AQEEPTQEEI PTHKENQPEE IQNEEIHVFE 550 560 570 580 590 600 EEPAFKHLAA QLSELVNMAE SSGQSGVGFQ PPVNAQPDVN MEGPAGYAPA TSQATWSNGV 610 620 630 640 650 660 NIPVKSANFR WKGPVGNFQL PSAQGKDGAM LVFGMNYSPE VFDRWASITR NYISSFNFND 670 680 690 700 710 720 GGDKIAWMED LLGETERKIF VSWRMRFKDE YQNLAKIANQ DGGTQAILSQ IRRIFLGEDP 730 740 750 760 770 780 VLGQNTVQNI AFRKLKQLVC PNYQSIRRYL MDYLTLAAET GLMWSETEGP AISEELFTKM 790 800 810 820 830 840 PAAIGERVAQ AYKIMDPTSA VNLPSRVYFT INYLTEQCKE ASYMRSLKAL DFCRDFPIEG 850 860 870 880 890 900 YYGRSGEKKK YTARKATKYT GKAHDNHIRV TKAKYQRKCK CYICGQEGHY ANQCRNKHKD 910 920 930 940 950 960 QQRVAILQSL DLKENEEVVS ADDKEEEDDE IFSVLGEEDY QEETIMVLEE DDIQQIIKEF 970 980 990 1000 1010 1020 SKFGDLSRRN VGPNFPGPAE VQMGVLKPKS SWRRPIQATL EEINCHHNWT AISTGQLACR 1030 1040 1050 1060 1070 1080 SCKQFLAGVQ CHHCHAVYCF MCAEAYHDVQ AEKILSKDYS FSARGKKGKA VIIEEDEIEG 1090 1100 1110 1120 1130 1140 EFLISQLQQE NQRLQKQVER LQEELMKLHR EKDEALKHSE KASRVFSTIQ ESDEAELNLI 1150 1160 1170 1180 1190 1200 KEELRQFKEE TRMAIAQLKE AIIVQEEDTI EERCAMILEE KHTENIYSAT AKAEYNGLYN 1210 1220 1230 1240 1250 1260 VKVGIKPDNM EPYYINAIVD TGATACLIQI SAIPENYYED AKVTVNFRSV LGIGTSTQMI 1270 1280 1290 1300 1310 1320 KAGRILIGEQ YFRMPVTYVM NMGLSPGIQM IIGCSFIRSL EGGLRIEKDI ITFYKLVTSI 1330 1340 1350 1360 1370 1380 ETSRTTQVAN SIEELELSED EYLNIAASVE TPSFLDQEFA RKNKDLLKEM KEMKYIGENP 1390 1400 1410 1420 1430 1440 MEFWKNNKIK CKLNIINPDI KIMGRPIKHV TPGDEEAMTR QINLLLQMKV IRPSESKHRS 1450 1460 1470 1480 1490 1500 TAFIVRSGTE IDPITGKEKK GKERMVFNYK LLNENTESDQ YSLPGINTII SKVGRSKIYS 1510 1520 1530 1540 1550 1560 KFDLKSGFWQ VAMEEESVPW TAFLAGNKLY EWLVMPFGLK NAPAIFQRKM DNVFKGTEKF 1570 1580 1590 1600 1610 1620 IAVYIDDILV FSETAEQHSQ HLYTMLQLCK ENGLILSPTK MKIGTPEIDF LGASLGCTKI 1630 1640 1650 1660 1670 1680 KLQPHIISKI CDFSDEKLAT PEGMRSWLGI LSYARNYIQD IGKLVQPLRQ KMAPTGDKRM 1690 1700 1710 1720 1730 1740 NPETWKMVRQ IKEKVKNLPD LQLPPKDSFI IIETDGCMTG WGAVCKWKMS KHDPRSTERI 1750 1760 1770 1780 1790 1800 CAYASGSFNP IKSTIDAEIQ AAIHGLDKFK IYYLDKKELI IRSDCEAIIK FYNKTNENKP 1810 1820 1830 1840 1850 1860 SRVRWLTFSD FLTGLGITVT FEHIDGKHNG LADALSRMIN FIVEKNDESP YRFTSSVEDA 1870 1880 LKVCNDDHGR NLISAVINDI ITVLRR

References

[1]	"Properties of Commelina yellow mottle virus's complete DNA sequence, genomic discontinuities and transcript suggest that it is a pararetrovirus." Medberry S.L., Lockhart Olszewski N.E. Nucleic Acids Res. 18:5505-5513(1990) [PubMed: 1699203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52938 Genomic DNA. Translation: CAA37110.1.
PIR	S11480.
RefSeq	NP_039820.1. NC_001343.1.
3D structure databases
ProteinModelPortal	P19199.
ModBase	Search...
Protein family/group databases
MEROPS	A03.004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1489554.
Family and domain databases
InterPro	IPR018061. Pept_A2A_retrovirus_sg. IPR001995. Peptidase_A2_cat. IPR001969. Peptidase_aspartic_AS. IPR002156. RNaseH_domain. IPR000477. RVT. IPR001022. TMV_movement. IPR013084. Znf_CCH_retrovir. IPR001878. Znf_CCHC. [Graphical view]
Gene3D	G3DSA:4.10.60.10. Znf_CCH_retrovir. 1 hit.
Pfam	PF01107. MP. 1 hit. PF00077. RVP. 1 hit. PF00078. RVT_1. 1 hit. [Graphical view]
SMART	SM00343. ZnF_C2HC. 1 hit. [Graphical view]
PROSITE	PS50175. ASP_PROT_RETROV. 1 hit. PS00141. ASP_PROTEASE. 1 hit. PS50879. RNASE_H. 1 hit. PS50878. RT_POL. 1 hit. PS50158. ZF_CCHC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POL_COYMV

Accession

Primary (citable) accession number: P19199
Secondary accession number(s): P19202

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	August 1, 1991
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program