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Database: UniProt
Entry: A0A091EEV7_FUKDA
LinkDB: A0A091EEV7_FUKDA
Original site: A0A091EEV7_FUKDA 
ID   A0A091EEV7_FUKDA        Unreviewed;      1731 AA.
AC   A0A091EEV7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Kinase D-interacting substrate of 220 kDa {ECO:0000313|EMBL:KFO33921.1};
GN   ORFNames=H920_04681 {ECO:0000313|EMBL:KFO33921.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO33921.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO33921.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO33921.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN122047; KFO33921.1; -; Genomic_DNA.
DR   STRING; 885580.ENSFDAP00000012508; -.
DR   eggNOG; KOG0502; Eukaryota.
DR   Proteomes; UP000028990; 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; 2.
DR   Pfam; PF12796; Ank_2; 4.
DR   Pfam; PF07693; KAP_NTPase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 11.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 9.
DR   PROSITE; PS50088; ANK_REPEAT; 10.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Kinase {ECO:0000313|EMBL:KFO33921.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:KFO33921.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        498..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        525..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        688..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          37..69
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          70..102
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          103..135
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          137..169
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          170..202
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          203..235
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          236..268
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          269..301
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          335..367
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          368..391
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          441..953
FT                   /note="KAP NTPase"
FT                   /evidence="ECO:0000259|Pfam:PF07693"
FT   REGION          1172..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1349..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1436..1537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1550..1577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1647..1731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1495..1527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1731 AA;  190884 MW;  6691220B6E916FED CRC64;
     MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMLAAEQGN LEIVKELIKN
     GANCNLEDLD NWTALISASK EGHLHVVEEL LRCGVDLEHR DMGGWTALMW ACYKGRTDVV
     ELLLCHGANP SVTGLQYSVY PIIWAAGRGH ADIVHLLLQN GAKVNCSDKY GTTPLVWAAR
     KGHLECVKHL LAMGADVDQE GANSMTALIV AVKGGYTQSV KEILKRNPNV NLTDKDGNTA
     LMIASKEGHT EIVQDLLDAG TYVNIPDRSG DTVLIGAVRG GHVEIVRALL QKYADIDIRG
     QDNKTALYWA VEKGNATMVR DILQCNPDTE ICTKDGETPL IKATKMRNIE VVELLLDKGA
     KVSAVDKKGD TPLHIAIRGR SRKLAELLLR NPKDGRLLYR PNKAGETPYN IDCSHQKSIL
     TQIFGARHLS PTETDGDMLG YDLYSSALAD ILSEPTMQPP ICVGLYAQWG SGKSFLLKKL
     EDEMKTFAGQ QIEPLFQFSW LIVFLTLLLC GLVGLLFTFT LDLSLGVAVS LSCLALLYIF
     LVVIYFGGRR EGESWNWAWV LSTRLARHIG YLELLFKLMF VNPPELPEQT TKALPVRFLF
     TDYNRLSSVG GETSLAEMIA TLSDACEREF GFLATRLFRV FKTEESQGKK KWKKTCCLPS
     FVIFLFLLGC IIAGITLLAV FRVDPRHLTV NAVLVSIASV VGLALVLNCR TWWQVLDSLL
     NSQRKRLHHA ASTLHKLKSE GFMKVLKWEV ELMARMAKTI DGFTQNQTRL VVIIDGLDAC
     EQDKVLQMLD TVRVLFSKGP FIAIFASDPH IIIKAINQNL SSVLRDSNIN GHDYMRNIVH
     LPVFLNSRGL SNARKFLVTS ATNGDIACSD APGLQEDADR RVSQNSLGEL TKLGSRTALN
     RRDTYRRRQM QRTITRQMSF DLTKLLVTED WFSDISPQTM RRLLNIVSVT GRLLRANQIT
     FNWDRLASWI NLTEQWPYRT SWLILYLEET EGVPDQMTLK AIYERISKNI PTTKDVEPLL
     EIDGDIRNFE VFLSSRTPVL VARDVKTFLP CTVNLDPKLR EIIADVRAAR EQINIGGLAY
     PPLPLHEAAP RAPSGCSQPP SVCSSSTSFN GPFAGGVLSP QPHSSYYSGM TGPQHPFYNR
     PFFAPYLYTP RYYPGGSQHL ISRPSVKTSL PVREQSSGLT VIQEDAAEGL PSPTDSSRGS
     GPATGPVLSL NSMNVDAVCE KLKQIEGLDQ SLLPQYCTTI RKANINGRVL AQCNIDELKK
     EMNMNFGDWH LFKSTILEMR NAENQAVPED PRLLPENASA AAAHGESARR SAHGAAELPH
     TELSGQAPYT LNFSFEELNT LGLDEGAPRH SNLSWQSQTR RTPSLSSLTS QDSSMEISKL
     TDKVQAEYRD AYREYIAQMA QLEGGPGSAA ASGRSSPHSA FDEARKPFLA KRADVLDHSS
     SGVSTSDASP LDPITEEDER AEQPGSKLLP GRKGAERPSL FQTELKLKGG GLRYQKLPSD
     EDESGPEESD HTPLLRESRD RRAEAQAPEL SAEPLRSLAK AKEFLSDALL DKKDSSDSGV
     RSSESSPNHS LHGEVAGGAR LERADLIELD DGGRGGLPDP GLARMSICSE DKQSPSECSL
     LASSPEEGWP ACHRAYNLNR TPSTVTLNNN SAPANRAGQV LDDTDGTRET SQVLLRPGPG
     PAALQNENLK SLPHRRGQRT SYARLPKEPS ELHSGAPADS AGFGEERESI L
//
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