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Database: UniProt
Entry: A0A2K5ATV3_CAEEL
LinkDB: A0A2K5ATV3_CAEEL
Original site: A0A2K5ATV3_CAEEL 
ID   A0A2K5ATV3_CAEEL        Unreviewed;       861 AA.
AC   A0A2K5ATV3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Tudor domain-containing protein {ECO:0000313|EMBL:SPC47538.1};
GN   Name=akap-1 {ECO:0000313|EMBL:SPC47538.1,
GN   ECO:0000313|WormBase:C56G2.1d};
GN   ORFNames=C56G2.1 {ECO:0000313|WormBase:C56G2.1d}, CELE_C56G2.1
GN   {ECO:0000313|EMBL:SPC47538.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:SPC47538.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:SPC47538.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:SPC47538.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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DR   EMBL; BX284603; SPC47538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K5ATV3; -.
DR   SMR; A0A2K5ATV3; -.
DR   EnsemblMetazoa; C56G2.1d.1; C56G2.1d.1; WBGene00016977.
DR   AGR; WB:WBGene00016977; -.
DR   WormBase; C56G2.1d; CE52511; WBGene00016977; akap-1.
DR   OrthoDB; 4118571at2759; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00016977; Expressed in larva and 5 other cell types or tissues.
DR   ExpressionAtlas; A0A2K5ATV3; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd22395; KH-I_AKAP1; 1.
DR   CDD; cd20407; Tudor_AKAP1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR047368; KH-I_AKAP1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047367; Tudor_AKAP1.
DR   PANTHER; PTHR22948:SF65; A-KINASE ANCHOR PROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|EPD:A0A2K5ATV3,
KW   ECO:0007829|PeptideAtlas:A0A2K5ATV3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          683..741
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          145..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   861 AA;  95717 MW;  8FE76E3BE99B744D CRC64;
     MVAAAAADAL AAGGDSSSPS DLYNKITGQQ SSTTTSLSYA ACDVITRHLI SMLLEISNWT
     NDLAKYLAGS EQSSDDGHNE RCLLFSSIFF AIDPSLALAQ MSSVASKHAL LIALGGFSIA
     ALFVWYINKK DKDGRKKKKV GDVISNGLPK TATASDVQTE NGNVKKANGH VNGDVQSSIG
     VSQKQQQKDE DEKTQKKDAV QNEKPSIDKK QPKSQAPTEK KEEKTVEIHT ETEETDHVAA
     GDSGVVSEHK EHDKKTKQKN DEPVSIDKKS EEIEVPKQAG VVNEEPKKQS EETVVEEQFV
     KKEEPKLKSA PTPLLTMPSK KKIPEEPTPT KMNDATSPLS LDIAAQMSPA SFSWSEEMEK
     SFNEEEFRLN ESSDIDRSPA SPLRHLQQQH NKNRSSQKRK GGRVNGRDGV HQPQQQHQQQ
     KKEEQGQIKK GQRRLTKEKS VEETPEKSQK RVVLKHHENE AGDAAHAQII ESPHHENASY
     EKSDSPGLDS QNSEASSQDS GRATGPLASP HEDGLTTEDD FLPMYEFEIP NSLVGLIIGV
     KGKTIKELSV RTNVRMLIRQ HHETDKVKTH QICQVRGKRD EINHCLQMLR RRFPPARFPE
     LNLQPVVPPV LPNSNFDMLS TQPTWLTLPE DIKCEVAVSS IISASHFFIQ QPTHPSFASL
     RHLDMYMGSL YGEQSNLPEL PIPCQNGLLC AAPVGNAWFR AVTVQYFDET DEVFVKFVDY
     GGYSKMARQD LRQIRTDLMS LPFQSTEVML AHVRPVDGTT NWSDAAMQKF RAMCIGKVIN
     CKMVGQSHDT RIPMVELYMM SKDGKDAQEV RFDQVLMNCG LARTADPSKM SRITVPAALD
     TESRMKRPSF SSQTSQTAVV C
//
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