ID G0MLV8_CAEBE Unreviewed; 938 AA.
AC G0MLV8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT36630.1};
GN ORFNames=CAEBREN_19896 {ECO:0000313|EMBL:EGT36630.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369}.
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DR EMBL; GL379801; EGT36630.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MLV8; -.
DR STRING; 135651.G0MLV8; -.
DR EnsemblMetazoa; CBN19896.1; CBN19896.1; WBGene00158621.
DR eggNOG; KOG1661; Eukaryota.
DR HOGENOM; CLU_312659_0_0_1; -.
DR InParanoid; G0MLV8; -.
DR OMA; ICIPINE; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF9; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1-LIKE PROTEIN; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT REGION 277..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 675..709
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 283..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 106678 MW; A0444951DB3B1487 CRC64;
MGNTESSNDA LVDRMITNRD IKHRRVERAF RTVERPYFLP KENRRYTTLP ERVEHPEGGV
FHPGPLHLSA LDIYAQVLDY LQIRRGDTFL NVGAGSGYFS TLVGVCLGDT GTNHGIELYP
NLIKYSQGTI KEWTMTASAS TVGFAPPDIR CADVHDHKFL DAHQHRYDRI YISFRLHDKA
VLFKVIKMLK IGGILVVPML QHMTRYTRLS ETEANCEVLA RVTFGEGKKF PEADMPEAPI
FERIPTLAYL SRQQLRRKCR QEAYSSLQTK AINKSLRIPV GGLPPEPSTP PEEPMEPSPN
VRPIPAALQQ TIFNLAGPEN IRGQDQPEAM FQRMRDDMLH MPRHIDFRDL IPGRHRTPRN
RRNIPSDEDD PMNDFNAGGE QVLLSTPSGE VYIPRPDISM IIIENAYGNH FINDAEEAIR
FDINEFLPRR RRPPPPPRAA DVPSASNAPP AHRPRRSLLD NPAYRTDHEG TPPAVPFDIP
FDSSDDSTTS SDEAPSGFSE SSSSSGPSTS GYRAARQMSE ERTPTPFPSP PPTVTSTSEQ
RGGVTERDID VYFSGSSNEP GSSTSSEEPE PRSSRRVTAP RDDEDNGTGS DSSSDSEPYQ
LERSMEDRIR AAMSGTFGRN ERRALRIATD PTASLFRAMI RESTEQPSTS SAATTSDTPR
PLMTEQEQEE IMRDADVALR RAADQERRME RMERMNADFA RRLREARRER VQRRAEWNMF
DLEAPIPPPR PERPPRHWRD TFNRRQPIAT RTVAGTRIEP DPESAHRQRM LHIRQTMEEI
EQRHFPTTPP TEEPPDEIEL SFDNDRVPRE EDGELTDDEE EVEPRRPRAE SALMSPGGFV
VHMGPPLSHE EMERRSHDLE EGNSMVQYMD DVAIRNINTP PEEDATLHES RQRARDERDL
EINYGNNAYQ RVVENLALPP ILIEYLVFAD MNIRPCII
//