ID A0A1S3HE08_LINUN Unreviewed; 625 AA.
AC A0A1S3HE08;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=A-kinase anchor protein 1, mitochondrial isoform X2 {ECO:0000313|RefSeq:XP_013383304.1};
GN Name=LOC106153753 {ECO:0000313|RefSeq:XP_013383304.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013383304.1};
RN [1] {ECO:0000313|RefSeq:XP_013383304.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013383304.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013383304.1; XM_013527850.1.
DR AlphaFoldDB; A0A1S3HE08; -.
DR EnsemblMetazoa; XM_013527850.1; XP_013383304.1; LOC106153753.
DR GeneID; 106153753; -.
DR OrthoDB; 4118571at2759; -.
DR Proteomes; UP000085678; Unplaced.
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 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 474..532
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 68358 MW; DD9475E5E1B83763 CRC64;
MELKGIVTVA VPAMATVLVV GLLWYTSRKK HKDEENKDKE EVGQVSVPKK VCPEEKDEND
LKIDTKIDAH EESNMVEENS SVCLPLKVSL SPNSNLETSA VCQSSPTLPV SGEPENEFDT
PEVATCNSIS ESVLTKGGSP VPVNEEVHSQ TMESALERSP SKSIKLRHNE LGCDTVDGGM
SGVNGEASSH ESGHSEHSDT SGCVGASSEV QIREEEFDSS ANGGGMNGLN ANNQIEKDSH
TSNGVMSSGV GNSCDLVEGH LTNGQLASGD KTCVEEKAPE HNVTGHGDGN THINTERNGD
SRKDNSPREN KKHDPHDIIR YEFEFPSELC GRLIGKHGST ITAIKTKSDT EISLSRQSYN
ETFQICAIEG TKDNVDYALK LIRRKFPKNQ FPNVDLRQLS THVQEASPVL APEMMQLTLP
EGVMVDVIVS SIVNASHIFV QQPTHPTYPS LERLNQFMIM CYQHDGIVPQ LPRPIEVGVI
CAAPMMDGWY RAQVVSVQDE TDECDIKYVD YGGYARIQAC ALKQIRSDFM TLPFQACEAY
LANITPLEGE ESYSLEASAV LEEVSQGRML QLQTLSAAAD GIPYVQLYTQ GAQGTLPILI
NRDLVDRGVV RWVENQENAQ LAVRD
//