ID A0A0V0Y1D5_TRIPS Unreviewed; 1377 AA.
AC A0A0V0Y1D5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Kinase D-interacting substrate {ECO:0000313|EMBL:KRX93991.1};
DE Flags: Fragment;
GN Name=kidins220 {ECO:0000313|EMBL:KRX93991.1};
GN ORFNames=T4E_811 {ECO:0000313|EMBL:KRX93991.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX93991.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX93991.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX93991.1};
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:KRX93991.1}.
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DR EMBL; JYDU01000079; KRX93991.1; -; Genomic_DNA.
DR Proteomes; UP000054815; 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; PF07693; KAP_NTPase; 1.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 9.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:KRX93991.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transferase {ECO:0000313|EMBL:KRX93991.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 508..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 51..83
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 84..116
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 117..149
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 150..182
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 216..248
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 249..281
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 282..314
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 315..347
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 348..380
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 452..949
FT /note="KAP NTPase"
FT /evidence="ECO:0000259|Pfam:PF07693"
FT REGION 1194..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX93991.1"
SQ SEQUENCE 1377 AA; 156102 MW; 74C1407D03DE8CB1 CRC64;
LNSMLTDARW TITSATSSTA KQDPFQVFEG GSYDNITSTF RNLPVDIANE KGETPLIISS
RLGDISLVKF FLQCGFDPNA KDDEMWNALL NAAKNGYIEI CKVLLDAGAN IEDSDVASWT
PLCWAVYKKR EDVVRLFIEK GASVNVIDEH TMTPLLWASG RGYTSIVDQL LRAGARVAVR
DGFGNDALIW GSYIKSLPIV QLLLKAGSCA DTVGMRGLTA LILATQANSF EMVKAILEKP
CALNAVDHKG HPALYYAVLN GNAEIVEALL NAGAYVNPSE QIRESVLLKA VKSGFIDVVR
LLLDHHVDID CQDSEGRTAL HLAIDKGFLE ILQLLLENEP NLELKNTDGD TPLLKSARIR
NLAFVQLFKQ AGANVGATDK NGDTSVHIAL RCRSRRMVQI LLAPPFDSRI LYQPNRNKET
AYSIDRAVGK PILPQIFGPL DSASKTEAMM GYELYSSALA DVLCAPNLSL PLFVGLYAKW
GSGKSFLLRK VRGALTTLSR SWLSPTPLIW SWSIAFLLNF ISIVFGLFLF TFLPWKVALW
PMLIIFATFF LTYLYIMKWK STLARRINMF ISRKYAFIRL TFQTMFFDPP VLNEREIFSC
PIGFIYADYR RLSNFECEHA LTNIIDTFYA GLESYYGWLP VRLARAFKTH SRGRRKPKPR
RLCGIPLMLL MALLVICFFV AVYLFLLYYQ KRFSGPFLLS LLILATVGLL SLYPTSFVVV
QSTVLRPRRT MKRLLSKIEK LSFEAFMEKL RTEVQILQET VDRLDCYTRS QTRMVIFVDG
LDSCEGSRIV QTLDAIQVLF GRSQASRFIV LISVDPHVVI AAVRNNLQSA FLQSEVSSYD
YLKLIIHMPL YLRNSEFVKL HQQLAQKQRR NAPVDTAGLK MLMRQETVAG SYWSLAESCR
GSMRSPKPSA IPSQTFLGPE IVRDDYFGDL NPRSLRRIVN ALSLTGRLMR AFDIDFSWVT
LGHWTSLIEQ WPYRMSWTIE YTERCGAADH VTLREMYNMI KDRIPNEHDY LIEMDRNPKG
LDSYFQSELD PVLCVHHMRT FIPFTSNLDP YVRKLIRDKL ETFDLTLNCP MIHHSEGVTN
ELLTVPVGVS RLFLHPMWRK VRLSTLTVME LCHLLKALPL SNIEAVEKYC RICHTSNISG
LTLSVCELDK LKTEFRMSFG DWEIFCLMVN YLRNREKQMD FSVENVEENA TLPQLIMKSS
STSTTSTLKR RKREDEDEAN TQHNWLQNRL GHLDKVDYEE EAVDIASSLI TNSRRSSVTF
EFDEVQSPEE GKKLSPYNNT LPQVAVSRLS PNTYANSEPL PSRPPSEAGK GQPSSATGEM
SRPLLSSSDS EEEEEEEEEE ENNQLTVRPK ETIFRPSILN SQNSLIRASS EPGVNVE
//
