ID A0A0V1HIZ2_9BILA Unreviewed; 1367 AA.
AC A0A0V1HIZ2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Vigilin {ECO:0000313|EMBL:KRZ09938.1};
GN Name=HDLBP {ECO:0000313|EMBL:KRZ09938.1};
GN ORFNames=T11_11147 {ECO:0000313|EMBL:KRZ09938.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ09938.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ09938.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ09938.1};
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:KRZ09938.1}.
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DR EMBL; JYDP01000066; KRZ09938.1; -; Genomic_DNA.
DR STRING; 268475.A0A0V1HIZ2; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd22417; KH-I_Vigilin_rpt14; 1.
DR CDD; cd22418; KH-I_Vigilin_rpt15; 1.
DR CDD; cd22407; KH-I_Vigilin_rpt3; 1.
DR CDD; cd22408; KH-I_Vigilin_rpt4; 1.
DR CDD; cd22409; KH-I_Vigilin_rpt5; 1.
DR CDD; cd02394; KH-I_Vigilin_rpt6; 1.
DR CDD; cd22410; KH-I_Vigilin_rpt7; 1.
DR CDD; cd22411; KH-I_Vigilin_rpt8; 1.
DR CDD; cd22412; KH-I_Vigilin_rpt9; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 13.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10627:SF69; PROTEIN BICAUDAL C; 1.
DR PANTHER; PTHR10627; SCP160; 1.
DR Pfam; PF00013; KH_1; 13.
DR SMART; SM00322; KH; 14.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 13.
DR PROSITE; PS50084; KH_TYPE_1; 13.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 216..284
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 288..356
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 361..428
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 429..494
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 499..567
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 571..640
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 645..715
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 719..788
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 793..863
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 867..936
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 940..1063
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1064..1130
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1142..1212
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1216..1286
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 53..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1115..1142
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 153753 MW; 26E0BA4D0819E13A CRC64;
MNPDISMMYS SPSLNMVSTD SLTLNGSPML GNTMDSLHVV TSCLGPVAQS APAFPVAPGA
EHSAQKQQQQ QQQQQHQHQQ QQQIQNQQPF IGSGTVEQNR KIVMDYEADF PKLATSTNAS
GPTLSALATT PAIRSTTVTQ IFQLPYEERK FRVKQDNQYG SNERNSEQIE CNEIMQKTAT
SIELCHNKDQ SITIVVSGKR QAVEEARKMI VQQLQTQANR ELRIPKQYHR MLIGKEGRRL
HLLEKETDCR IVVPNRNNSS DVIKVIGPRE GIEKAIHKIQ IFVDEQSKLA SENLIIPKIY
YPWIRGPDNA VVDRIKQETG VSVHIPPPSA NNEVIVVTGE KEGVYKAVAQ IREIYEEKQR
SCRTVTVSVA PSQHSYVMGY QRSGITEILR DTGVSVEFPA DEESPEITLR GHPDQLGYAV
AMVYAKASSI VTARVNCPTW LHKFIIGSKG SNLKAIVGDF LKVHVTFESE GFIFLEGPPQ
DVERVKQLLN DRVTALENEM ATDVVIVHPS LHGHIIGKNG LNIVRIRQEF EVNVIIPDPG
SHSSEVRLEG KKAGVVKAKE EIQLLAEKKE NEKIRDILID SRFHRMMIGV KGEHVRDLRQ
RFPNVVVNFP DQGRKSDVVS LRGPKNEVDA CYGVLQQMYR ELLESKHQVR VPIFKDFLKH
IIGKGGANIK KLMEETGTKI EIPSDENSNE SNVILITGKK SDTAKAEKML QKMQSELANI
VTVELNIPRK LHSSLIGSGG RLIHSIGEEC GGVQIKFPAE NAHSDMVTVR GPKDGVDKAK
KVLLDLVKDR EASSFTAEVK TRPELFGFLI GSGGSRIKKM RESFPSVRIL FPRPCDDDKE
TIHLIGKKND VLNAKKQLDD WISELNRSVE IAVNIDPKWH SHFLSRSRSV LRDIQEQFGG
IFISFPKLAS GNGRVTLKGP KECVEGAKVQ LLDIVTKLES QVTEGVHIDP RHYKVLLRNR
GAFVQEISHQ YEVQIKFPDR EQQQHQQQQQ KQKQQQQQQH ANNNHATTNS TANWNGTCDG
SDGENARASS PAVVDQPLND LVLVTGQPDK CKKVIQLLLA EIPVTEVIHV PVEFHRGLIG
RQGSEIRRLI EAYDVNVHIS PPEQSLDEVV VIGKASSVNQ AVEAIKQHVA QLEREVKDRE
LKSFALQLSI PCALVPKLIG IKGREIQRLR SKYDVLISVP QQRADDGDTE VTITGYEENA
TNCKKEIETM VADYKSLCTQ EIALDCRVHN RIIGQRGKNV KRIMEQYQVE IRFPRQADQN
PNLVTVCGKV EDSVFDCIDH LRNLEEEYLQ DIVDRYAYRD PMRMAEENTT AQHQPAIEIV
NAPWQRTQTD DELSKPVPDV ENMQEFPSMV SDLPQSQMNA SVWNFKR
//
