ID A0A067E1B3_CITSI Unreviewed; 796 AA.
AC A0A067E1B3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ribonuclease P {ECO:0000256|ARBA:ARBA00012179};
DE EC=3.1.26.5 {ECO:0000256|ARBA:ARBA00012179};
GN ORFNames=CISIN_1g002846mg {ECO:0000313|EMBL:KDO48868.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO48868.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO48868.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000928};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily.
CC {ECO:0000256|ARBA:ARBA00007626}.
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DR EMBL; KK785128; KDO48868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067E1B3; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11980; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR002885; Pentatricopeptide_rpt.
DR InterPro; IPR033443; PPR_long.
DR InterPro; IPR031595; PRORP_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00756; PPR; 1.
DR PANTHER; PTHR13547:SF7; RIBONUCLEASE P; 1.
DR PANTHER; PTHR13547; UNCHARACTERIZED; 1.
DR Pfam; PF17177; PPR_long; 2.
DR Pfam; PF16953; PRORP; 1.
DR PROSITE; PS51375; PPR; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 182..264
FT /note="Pentacotripeptide-repeat region of PRORP"
FT /evidence="ECO:0000259|Pfam:PF17177"
FT DOMAIN 363..508
FT /note="Pentacotripeptide-repeat region of PRORP"
FT /evidence="ECO:0000259|Pfam:PF17177"
FT REPEAT 421..455
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT DOMAIN 553..776
FT /note="PRORP"
FT /evidence="ECO:0000259|Pfam:PF16953"
FT REGION 64..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 90069 MW; ADD8C06CDA04981A CRC64;
MASSLTVNTL QQQNQLFSLT LCKSSPPTLT VFNFQFLSRF LSSSPPKRTP LLVFKAHVRN
TQAKLSTTET EHETSTVTLR TRKGTASGAS SLGTRDKRVD SAGEEKDGKR LTKDNNSRKN
FAFLKSREMS SGNSSLRSKD KKIGIKSSKT VNREVDNQKM EQRTNDSGQY KVRGITDEKG
SKKSKKDRSE QFQLRVELDM CSKRGDVMGA IRLYDKAQRE GIKLGQYHYN VLLYLCSSAA
VGVVKPAKSG SGMRTLDTFE VSTMNSTELG DSRDMDNNGQ LDYGSSPMID KLESNSSYRF
DDLDSTFNEK ENLGQFSNGH MKLNSQLLDG RSNLERGPDD QSRKKDWSID NQDADEIRLS
EDAKKYAFQR GFEIYEKMCL DEVPMNEASL TAVGRMAMSM GDGDMAFDMV KRMKSLGINP
RLRSYGPALS VFCNNGDVDK ACSVEEHMLE HGVYPEEPEL EALLRVSVEA GKGDRVYYLL
HKLRTSVRKV SPSTADVIAK WFNSKEAARL GKKKWNESLI KDTMENKGGG WHGLGWLGKG
KWIVSHTTVG GDALCKCCGE KLAIIDLDPI ETEKFAESVA SIAIKRERNS SFQKFQKWLD
YYGPFEAVVD AANVGLYSQR NFKPARVNAV VNGIRQKFPS KKWPLIVLHN RRITGHKMDQ
PVNRALIEKW KNADALYATP TGSNDDWYWL YAAIKFKCLL VTNDEMRDHT FQLLGNDFFP
RWKERHQVRF SFSDAGPEFY MPPPCSVVIQ ESEKGNWHIP IASKQDYDDE ERRWLCVTRA
NSHMNRQNSY SSPKAS
//
