CK5P1_CAEEL
ID CK5P1_CAEEL Reviewed; 547 AA.
AC Q09316;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=CDK5RAP1-like protein;
GN ORFNames=F25B5.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Potential regulator of CDK5 activity. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00780};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|PROSITE-ProRule:PRU00780};
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC subfamily. {ECO:0000305}.
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DR EMBL; FO081045; CCD68781.1; -; Genomic_DNA.
DR PIR; T16145; T16145.
DR RefSeq; NP_498290.1; NM_065889.5.
DR AlphaFoldDB; Q09316; -.
DR SMR; Q09316; -.
DR STRING; 6239.F25B5.5; -.
DR EPD; Q09316; -.
DR PaxDb; Q09316; -.
DR PeptideAtlas; Q09316; -.
DR EnsemblMetazoa; F25B5.5.1; F25B5.5.1; WBGene00017776.
DR GeneID; 175841; -.
DR KEGG; cel:CELE_F25B5.5; -.
DR UCSC; F25B5.5; c. elegans.
DR CTD; 175841; -.
DR WormBase; F25B5.5; CE01922; WBGene00017776; -.
DR eggNOG; KOG2492; Eukaryota.
DR GeneTree; ENSGT00940000165667; -.
DR HOGENOM; CLU_018697_2_1_1; -.
DR InParanoid; Q09316; -.
DR OMA; CEHFHIP; -.
DR OrthoDB; 835984at2759; -.
DR PhylomeDB; Q09316; -.
DR PRO; PR:Q09316; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017776; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035597; F:N6-isopentenyladenosine methylthiotransferase activity; IBA:GO_Central.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.12160; -; 1.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006463; MiaB_methiolase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA; 1.
DR SFLD; SFLDG01061; methylthiotransferase; 2.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00089; TIGR00089; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..547
FT /note="CDK5RAP1-like protein"
FT /id="PRO_0000141767"
FT DOMAIN 79..194
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT DOMAIN 218..475
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 478..543
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 236
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 239
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ SEQUENCE 547 AA; 61315 MW; 83FD2D11A3DB483B CRC64;
MLRQWWLRSV GSCSTVYRAH SGCSTSAAVK PKRAIPTDGL QLSDFIKEST KKQRQKAIIP
SIEDTKEYLN PEDLQGNGRT VCYVTYGCQM NVSDMEIVRS IMTKYGFVES DKKENADIVL
LMTCSIRDGA EKKVWNQLKL IRSNSVNKGQ IVGVLGCMAE RVRHDLLEKR NLVNIVAGPD
SYRDLPRLVA VAAGGSNGIN VQLSLDETYA DVQPIRVDSA SKTAFISIMR GCDNMCTYCV
VPFTRGRERS RPIESIVEEV QRLRDQGYKQ VTLLGQNVNS YRDMTSMDFS MAPSTSQEDR
VPGFKTVYKP KSGGLTFTTL LEKVADAAPD IRFRFTSPHP KDFPMQLIEL IASRPNLCKQ
LHLPAQSGDD ETLERMERGY TRDLYLRLVD DIRHVLPSVS LTSDFIAGFC GETEQAHQNT
LSLIRAVRYS FCFVFPYSMR GKTRAHHRLT DDVPEDVKAR RHLDLTTVFR EEALKLNQAL
IGSEQTVLLE GKSKRDASFS HGRIDGGVKA VFDNSKLCLE PGQYAKILIT DANSQTLKAQ
LIGQSSI
