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Database: UniProt
Entry: A0A1Q9EFE2_SYMMI
LinkDB: A0A1Q9EFE2_SYMMI
Original site: A0A1Q9EFE2_SYMMI 
ID   A0A1Q9EFE2_SYMMI        Unreviewed;       848 AA.
AC   A0A1Q9EFE2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Ankyrin repeat domain-containing protein 17 {ECO:0000313|EMBL:OLQ06152.1};
GN   Name=ANKRD17 {ECO:0000313|EMBL:OLQ06152.1};
GN   ORFNames=AK812_SmicGene10613 {ECO:0000313|EMBL:OLQ06152.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ06152.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLQ06152.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ06152.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-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:OLQ06152.1}.
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DR   EMBL; LSRX01000166; OLQ06152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9EFE2; -.
DR   OrthoDB; 1063832at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd17039; Ubl_ubiquitin_like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   PANTHER; PTHR24188:SF29; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24188; ANKYRIN REPEAT PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF00225; Kinesin; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817}.
FT   DOMAIN          1..57
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REPEAT          94..126
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          128..160
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          161..193
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          195..227
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          228..254
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          457..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   848 AA;  92819 MW;  44DB81C00C96DF0C CRC64;
     MLRIKMLSGE ALTSIPVEEV HDVRGLKQCL NQQHGLPPRF RQRVLLHGEM LEDTATLHSP
     KDLHLVVLAF ADVSQSEVES TLQLPANPNS LNSDGFTALH RASECGHAEI VHLLVEAGAD
     KDVRDDCGGI TALMHASYNG HVEVVRLLVE AGTDKDDTDD RGCTALMHAS RNRHVEVVRL
     LVEAGADKDV RDDCGGITAL MDASFNGRVE LVRLLVEAGA DKDVTDEHGC TALMHASCNR
     HVEVVRLLVE AGADKVGAHN DVAKVDQRSN SDRAHELRIA AGLGTFPERY VANPPDWWNE
     GGRSPSLWLS WHMAKELEGA VLYWGPNRGV GQDNLGLVAD RPEMRMLAGY HSKTGAHGPQ
     KKLQGAFGRK DLQLQTFAVR GAKRVAIASE EEGLHQYFVG DTHRTVAETP HNLNSSRSHC
     IFTIFIEAFA TELVEALVRR VGDGSVCCWR RVGGLGQRTK GGKEGGKEER KEGRKEGRKK
     GRKEEGKEGR KEGKKEGRKE GRKEGRKEGK KEERKEGKKE EGKKESRKGG KAMKGFKGGK
     GKGKGKEKME SKGQGKGGMM RPPNTSPAWG LSAAVARDDK MYVGAAASSG PFGKPYEAGS
     QNSRVLMGQA VSINLSLHML ESVINALNKK SGMVPYRNSF LTKALKDALG GNARAVMGDL
     EPKATFCDSS KKAMLEALSF AGETPLAAEL RQVWSNDLLA FQAPTARLYR RQVVRGPVGT
     SSLKFELHNY GSRTISLDDP RPGVVVPAHS LRSLNATFDT LAIDCEGCFG SFLAENPDLL
     EMLSMIVVEV HGDPGPEQEA VDKLISEGWE LKQRLRRQRV LCKGPCESQC DLVWVAQHAH
     QYWGEDLW
//
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