ID A0A0V0X9L7_9BILA Unreviewed; 1397 AA.
AC A0A0V0X9L7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Kinase D-interacting substrate {ECO:0000313|EMBL:KRX84307.1};
DE Flags: Fragment;
GN Name=kidins220 {ECO:0000313|EMBL:KRX84307.1};
GN ORFNames=T06_5 {ECO:0000313|EMBL:KRX84307.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84307.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX84307.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX84307.1};
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:KRX84307.1}.
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DR EMBL; JYDK01000007; KRX84307.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011646; KAP_P-loop.
DR PANTHER; PTHR24116; KINASE D-INTERACTING SUBSTRATE OF 220 KDA; 1.
DR PANTHER; PTHR24116:SF0; KINASE D-INTERACTING SUBSTRATE OF 220 KDA; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07693; KAP_NTPase; 1.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 9.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:KRX84307.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transferase {ECO:0000313|EMBL:KRX84307.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 514..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 544..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 57..89
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 90..122
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 123..155
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 156..188
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 222..254
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 255..287
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 288..320
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 321..353
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 354..386
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 458..955
FT /note="KAP NTPase"
FT /evidence="ECO:0000259|Pfam:PF07693"
FT REGION 1231..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX84307.1"
SQ SEQUENCE 1397 AA; 158285 MW; EA845E1525927D6E CRC64;
LNSMLADAPY TNFEMWTITS ATSSTARQDP FQVFEGGNYD NITSTFRNLP VDIANEKGET
PLIISSRLGD ISLVKFFLQC GFDPNAKDDE MWTALLNAAK NGYIEICKVL LDAGANIEDS
DVASWTPLCW AVYKKREDIV RLFIEKGASV NVIDEHTMTP LLWASGRGYT NIVDQLLRAG
ARVAVRDGFG NDALIWGSYV KSLPIVQLLL KAGSCADTVG MRGLTALILA TQANSFEMVK
AILEKPCAVN AVDHKGHPAL YYAVSNGNAE IVKALLEAGA YVNPSEQIRE SVLLKAVKSG
FIDIVRLLLD HHVDIDCQDS EGRTALHLAI DKGFLEIVQL LLENEPNLEL KNADGDTPLL
KSARNRNLAF VQLLKQAGAN VGAVDKNGDT SVHIALRCRS RRMVQILLAP PFDSRILYQP
NKNKETAYSI DRAVGKPILP QIFGPLDSAS KTEAMMGYEL YSSALADVLC APNLSLPLFV
GLYAKWGSGK SFLLRKVRGA LTTLSRSWLS PSPLIWSWST AFLLNFISIV FGLFLFTFLP
WKVALWPMLI IFAAFFLTYL YVMKWKSSLA RRINMFISRK YAFIRLTFQT MFFDPPAMNE
REIFSCPIGF IYADYRRLSN FECEHALTNI IDTFYAGLES YYGWLPVRLA RAFKTHSRGQ
RKPKPRRLCG IPLMLLMALV VICFFAAVYL FLLYYQKRFS GPFLLSLLIL ATVGLLSLYP
TSFVVIQSTV FRPRRAMKRL LSKIEKLSFE AFMEKLRAEV QILQETVDRL DCYTRSQTRL
VIFVDGLDSC EGSRIVQTLD AIQVLFGRSQ ASRFIVLISV DPHVVIAAVR NNLQSAFLQS
EVSSYDYLKL IIHMPLYLRN SEFVKLHQQL AQKQRRNATV DTAGLKMLMR QETVAGSYWS
LADSCRGSIR SPKPSAMPSQ TFMGPEIVRD DYFGDLNPRS LRRIVNALSL TGRLMRAFEI
DFSWVTLGHW TSLIEQWPYR MSWTIEYAER CGAADHVTLR EMYNMIKDRI PNEHDYLIEM
DRNPKGLDSY FQSELDPVLC VHHMRTFIPF TSNLDPYVRK LIRGMFVFYI SNFFNFISLY
QKNMHIDKLE TFDLTLNCPV VHNSENLTNE LLTVPVGVSR LFLHPMWRKV RLSTLSVMEL
CQLLKALPLS NIEAVEKYCR ICHTSNISGL TLSVCELDKL KSEFRMSFGD WEIFCLMVNY
LRKREKQMDF SVENVEENVA LTQLIMKSSS TSTTSTLKRR KQNEDEANMQ HNWLQNRLGH
LDKVDYEEEA ADKASSLITN SRRSSVTFEF DELQSPESGK KLSPYNTMPQ VTVSRLSPTT
YANSEPPPSR PPSEAEKGQP SPVSGEMSRP LLSSSDSEEE DNNQLTVRPK ETIFRPSILN
SQNSLIRASS EPGVNVE
//
