ID A0A162T8R6_9CRUS Unreviewed; 2138 AA.
AC A0A162T8R6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Kinase D-interacting substrate of 220 kDa {ECO:0000313|EMBL:KZS22002.1};
GN ORFNames=APZ42_010848 {ECO:0000313|EMBL:KZS22002.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS22002.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS22002.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS22002.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS22002.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) 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:KZS22002.1}.
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DR EMBL; LRGB01000005; KZS22002.1; -; Genomic_DNA.
DR STRING; 35525.A0A162T8R6; -.
DR Proteomes; UP000076858; 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 Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011646; KAP_P-loop.
DR InterPro; IPR013761; SAM/pointed_sf.
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; PF00023; Ank; 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 SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:KZS22002.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KZS22002.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 927..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 306..338
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 339..371
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 372..404
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 405..437
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 438..470
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 471..503
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 504..536
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 537..569
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 570..602
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 603..635
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 709..1274
FT /note="KAP NTPase"
FT /evidence="ECO:0000259|Pfam:PF07693"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1890..1924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2114..2138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2138 AA; 236682 MW; FCBAF010256CB56B CRC64;
METNRLCLME ASAKSQPSPK TGSVKGRSHS LTTVLPLPLV RITPSVEEET EAGGSESEPT
LNHPSLPISD ATKRILEKKP TAKHRPRLSI PHIFTNQSSL STSPLSSTPS ISSLLSAAAA
ARNFSFSIPH SMRRGSWSVS LLSDRAKNKN HRMDSFLLFP SAPCIYSWKP TTPHWNKIDH
VLHGSPNGSK CKQKNRENAC MLVRHPNLKP QFSDLGRCEC LLILLDNYLT SDIFVITKFH
VHFWHEVDIS RPFSRQFINM RIENPLESMV SLSYRTFANY IVEDNLIGLR VFLENRHVVV
DDRNENGATA LVLASIKGKS AFVKELLAHG ADPNAEDSDN WTPLLCAAKE NFTSICVELL
NHGADIEHRD MGGWTALLWA SYKGYLETAR LLIEQRAEVN VHGQFHITPL MWAAGRGHVA
IVRLLLENGA KVNAGDKYGT TALIWACRKS HGEIVDMLLQ AGANVEVSGM HCWTPLLLSA
KENAADIVNK LLDRKPNVNA TDKDGCAALT LACKEGYYDI CMALLNAGAY VNLQDRSGDT
NLIHAAKAGH KSIVEALLKK YADVDMTGKE RKTALYWAVE KNHVSVVKSL LNSDPNLEIS
TKEGDTPLLR AVRNRSIEIV QLLLDKKARV TAADKEGDTV LHIAMRARSK AIVEVLLRNP
KHSQLLYRPN RSGETPYNID ISQQKTILGQ IFGARRLNTN EDNENMLGYE LYSSALADML
SEPSLSMPIT VGLYAKWGSG KSFLLSKLRD EMKGFARQWI EPQLQFSVVL SIIVLHIATL
LGVIMGVSLD SWIAGLATGG GCFFLIVTFL YIVYWGSERF SWNWAHSFGL VLARKLEALK
LVLQVTFCTP PGPQWGGDSI RIQPIRFYFT DQTKVSRSTR GENSVVQMIG SLLDSIEGDY
GVVATRLYRA FRPKPLKSTS PWKFRRFCCI PYAAIFLICI DILLAGLVFL AIYQNAEIED
RIVNSNHVQY TLIAIGVFLG VVIIANGYTW GRIVKSLLFS QRRKLLRIIG RLQSVRAEGY
LQALKREVAI MVEMVRCLDA YSGQQTRLVM VVDGLDSCEQ DQVLYVLDAV HLLFTEQSSP
FITLLAIDPH IIIKAIELNL HRMFNESNIG GHDYLRNLVH VPFFLQNAGL RKVKAAQQAA
LMLKNPGGVR TMVTSNSNHA AVLNWLESED TANNQPAGDK VVMSPRRMSV ESSAPQGKGL
HRNHKLSSAL PPAMGHRKLR PSESMESGLA MGNNNRVMAA QDLTKVLLTD DYFSDVNPRS
MRRLMNVIYV TGRLLKAFQI EFNWYHLASW VNITEQWPYR TSWIILYCEV NEDKLDDLTT
LKVVYERAKP FIPVSKEIEP HLEIDRDEKK FQTFLSFHRN TLQVLHLKMF MPFTIHLDPY
LRKVIKEERS SFMAMQSGAP VPHTATADVK VNGNIIHEQP NPSVGMHVPW SVNGQPWTTV
TLPTPDQNKP TMYPKYPSMV PTITHCNYGV MPATAYGPAV NQLCLKSTLP SRLQDRSLSS
LTAEEVSELL RHLDGFRTAQ ADQYTRTFID NNISGRVLLS CNLDELKALS GMSFGDWELF
RVAVCALRER EFQPRVANSP NPQQATAGQT STTQHQSGNY NFLDVDFEGR LSRSSSLRSN
TFAGTAPGEV VSEVDAIISA PKINTKRQTN IEKQVTLEDQ AICGALQTLN EEAMEDVLDE
REAEYLPGND LMPNVYGYNS SNLSTCSDPT ETDVLYLQTS VVPDLHFPAL RHANSVLGSR
GLIGNEDSVS LGSSLVSLAE RGTVTPARQR TITEVVWPEQ IASALNSGLR SRLSSSTSLF
RAGSQKSILA SDASYALSRR DSQRSVSDVG STKPIFVSVD PSNIAESSCP VSSGFSPSVA
GGWRSEQGSP RRPASLVFNE TVNPTHDWLV KPVRDTPESP TGENRLKCTS GDRTPTASSS
SPIIVHKRFS TTNVELLPDQ IAGKLQPDKM TSSKSALRSP SKQRARRTGH HQSRTHVVPS
PGLSTSRHPS GKSSDDTDED GEDAPLMAAK EYVHHVRRVL PKATVLAIKE SRPLSANSSF
LGNYVQQTEG GGVANTTSSQ LSLASPIGSS TSSLDSPLDT TDNEVYKTVI PKGDSSRREN
SLALMLNRAI NEIGDTGRAM ATPSKPEPSA SSEMETAN
//
