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Database: UniProt
Entry: A0A1R2AT74_9CILI
LinkDB: A0A1R2AT74_9CILI
Original site: A0A1R2AT74_9CILI 
ID   A0A1R2AT74_9CILI        Unreviewed;      1682 AA.
AC   A0A1R2AT74;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Tetratricopeptide repeat protein 29 {ECO:0000256|ARBA:ARBA00040665};
GN   ORFNames=SteCoe_35043 {ECO:0000313|EMBL:OMJ67717.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ67717.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ67717.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ67717.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Axonemal protein which is implicated in axonemal and/or peri-
CC       axonemal structures assembly and regulates flagella assembly and
CC       beating and therefore sperm motility. {ECO:0000256|ARBA:ARBA00037175}.
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:OMJ67717.1}.
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DR   EMBL; MPUH01001447; OMJ67717.1; -; Genomic_DNA.
DR   OrthoDB; 927920at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 8.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR46630; TETRATRICOPEPTIDE REPEAT PROTEIN 29; 1.
DR   PANTHER; PTHR46630:SF1; TETRATRICOPEPTIDE REPEAT PROTEIN 29; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   Pfam; PF13181; TPR_8; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 16.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 6.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50005; TPR; 5.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          221..254
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          470..503
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          511..544
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          921..954
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1126..1159
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1340..1680
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   1682 AA;  199886 MW;  4BC699CBC94A821A CRC64;
     MSFTGNKITD EAKALELLGD NEYRVGNFQV AHSFYLKAYD INRNPGDLRL YFKITETLFS
     TCIQLYQISL SDLKIPKKCS KLCLKMMQGR KYDQILLDKL NLIKLCYYIK AKKDDKAIQL
     LHFFNSIESN FNSKIFFETY IGISRFLLMN NEIEEALKTL KKCSKVNKNI LKTNYQNQGF
     IYYLLGGIYF DLNNNEKSSK NYIKFLNLYE RELFTDIIFV SEGYLYLALL YVKINSNEKA
     IENFEKCKNI SKNMENPDLD TLKLIYHNLS ELYNKMNDKQ KSFEEIEKYV EVLQLISPDH
     PELESKYIFI VESYCSLNNF QKQLEYYKKF KKLMIRKLGP KHEILTQVYF YIGVLYNLNN
     MPQKVSKYYN KLLVLLENTP DGDKNKLLYA YFYFGLLSNS LGENKAWGYF KKCRKILREN
     PGLINEKFTI TYIKLGKYYL IRKAEKAVKC LEEYHIFRKD LIKYKYNHLI DLYITLGLAY
     KNIEEKEKAI EEFEKCRQEL NKDSLNNSLF YEKYFNLGKL FSDLKENSKA VDCYNKAIEI
     YKKNNNLFTY FDTVCEAYME IIELLAKMND KEKIVFYCKD FKGKLKKIMK SDHSNLELSY
     YYLGCLGEIA NKINKAQKYF KESIELARKS KNYVLLSRVY MKLGILYFNE HNKNNENIKK
     TFEYFKLCLK LKIKFKLYDT KLAEVYLYIG KLYLIKNKPI KAEKMFENCR KLSEKILTPN
     DYFIASVYYC IGLMHFSNAK GAIEFLEKSR SITENIYSDR HTDLLLIYKH LSIEYYHINN
     YKKSIKYSEK CKNLINSFSS PDKLSLMEIN SFLFKLYIDT NDFEKLNSLN MEILQSSFFD
     SLSVLFSKVF ITKFSLFKYN VRFLNSIEEI IGSNHQSLQS FYLEVGNLLI YANLYNEALV
     YYEKYMNISK KFFKPNSISL ANAYFCLGNT YISLKNKPKA IKFFEKSQQL LENYYPKNYF
     ALFQNYELLE RLYQEINEHT KAAENFRKRK YFEQNYKKQL DLGKNNFIQT LNIFTQILQK
     LINSNQNIIQ NIISFLSNIP SINYDMISMV YDTIESVKTS YFSVKLKEDF EDNTTGFLNE
     FSREKQLFNY GLIYDLSSDF KNAIKYYEKC KEEREKKMGE NHSDLASIYN LLGNVYFEVG
     EKKNALVYYE KCRNIKEKLD PMNIDLVIIY NCLFYLYSDS NEPRKAKEFL NKSLEIKKKS
     QIVQKNAFFM IVKFFYNIEY FISDLNFMKI IRNLYSVCKK IKENKISRDD PYLKLDLNLH
     LELISDKLDM KNKFENSLVI IEFIEYCLFL PKCINNNRQA IIGLSEIFEH IDQKKNINAS
     NLMTDNIKKY LLNYFNIPNE KKSSTQHEKS FSLVKHKRDK DYLYFESDKK LIVPFKNCPK
     FFPNIYNKSL SYFKNIDKKK KSLKIFEKKY KGIYGDWKYI NSIYKEIKFL KMILKKNPIV
     PSVYYFRLIK TDSANILLGV NDCGDNLKNY VANPNNHISE REAKILLFNI MKAYNTLYEN
     KIVHSDVSPY NILVKSPEKV FLCDFSDSFI CTEVTENNPF PTIWPKKNVT VDFLSPEKKS
     WSILFGSNPI SYDPFKSDVF SIGLCFLNSF GVDIKNLNDY DDSFYGYIYE ILMNGYDNFV
     KDSLRRFSFK LLRNRLQKNI DEIVDEFPLE SLREILKNML EVDMAKRPSI RHVYKKAESM
     GL
//
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