ID A0A0V0WJ04_9BILA Unreviewed; 627 AA.
AC A0A0V0WJ04;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=KH domain-containing protein C56G2.1 {ECO:0000313|EMBL:KRX75674.1};
GN ORFNames=T06_7964 {ECO:0000313|EMBL:KRX75674.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75674.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75674.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75674.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX75674.1}.
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DR EMBL; JYDK01000117; KRX75674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WJ04; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 478..542
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 134..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 69889 MW; 41EBC3EC14CAB5F2 CRC64;
MKASFLNIFY RRLYFGCRSA WYRRASVRNK VAGGTGQRRA KQGICRLNQA YSMPIVFPPF
SRQVCLVGSV ACLTSASAAY LFYCWKKFVQ RAEKFASVDQ AEVVVVDQGD KLGNNNPAPI
SECEVTVPLN HNSTEKPIMS YKRGGRVNHR KASLKAATGN GNQKSPEVNV EDPVAVPVVN
GRQNPTNGTE AKERANNERR SEENFPSENR SDYYSSSNGD SEGNSTNGTP NVFYNGGFVN
GQYNGSERNF YDGNNRENAY RAAPSVCTEL SVRVMSYSTV TGPCSRGSME SFPSASSSVE
ASNNAWRGSA AESGYTSVQS SHFGEKKEYN FEIPANLVGL LIGRSGINVK RIQELSGSKI
WINSHCFKDG SKICTIRGDR DAINNALRAI RKRFPSSMYP MLKLTPLLFV DSFHLPAEKF
LDLELPVDVP IETTVCFIQN AVHFFVQQPT HPTYLMLSEF QANLNNAYNA NECSLLIPEP
VGGNMVCVAS FDNVWYRVMT LGTAEVNENG ENEIWIRILD FGGVLKSPVW NLRQIHAEFL
NYPFQATEVF LSNVKPVNEE IGWTQESLEL VRQFTANKIV HTCSVFGPSY SGQRFVEVFL
FDMEITLSTL LVSNCCAEWI IPPQLTQ
//
