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Database: UniProt
Entry: M7C1C2_CHEMY
LinkDB: M7C1C2_CHEMY
Original site: M7C1C2_CHEMY 
ID   M7C1C2_CHEMY            Unreviewed;      3286 AA.
AC   M7C1C2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=TPR and ankyrin repeat-containing protein 1 {ECO:0000313|EMBL:EMP38178.1};
GN   ORFNames=UY3_04610 {ECO:0000313|EMBL:EMP38178.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP38178.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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DR   EMBL; KB520471; EMP38178.1; -; Genomic_DNA.
DR   STRING; 8469.M7C1C2; -.
DR   eggNOG; ENOG502QQZC; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR039904; TRANK1.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR21529; MAMMARY TURMOR VIRUS RECEPTOR HOMOLOG 1, 2 MTVR1, 2; 1.
DR   PANTHER; PTHR21529:SF4; TPR AND ANKYRIN REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT   DOMAIN          977..1440
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          2993..3250
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          592..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1215..1237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2716..2737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2919..2949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2269..2296
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        592..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1085
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2921..2949
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         998..1005
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         3022
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   3286 AA;  376934 MW;  C195B721DF8CE2C5 CRC64;
     MDLMNYAEFM KKAGNENFKN GNYFMAIRNY DEAIRVLFQL FQWGMVSHRD VAVLLCNKSN
     AFYSLGKWEE AYHCAKESLQ WDLSYVKGYY RSGYSLLRLS RTHDAVIMFS RGLTLLCGSV
     DQSQIADFIV GIFTSVNDEK YIAPYFLPIF KNIVNERFDP LVWQAVIEKL AKKGMWQKYV
     LFGQYERMER VPELVEWLIT IGANVGSIGA YPLHAIINLC IKASQTENVQ MLLNTGVDPT
     IPDAQARCAA DILKKTKNFK AVDIINNHLA RHASSSKESP GKSKSKASVD ETNSFLDAFE
     QFLMFCSPEN QAQHKNLLKH ETVQRFLKLL STVKEIPKEM VCDIYDTCAS SFIKLLLEKQ
     MWHEVLLLLT RKANGEMPSC GGLIRNCSLS DLNIGSVIKQ VDRRDKRRVH LVRCLLERGA
     SPEGTGAIPE KPLQICLKNN DFELAYLLLS RGADTRSVSI VEGDTPLHAA VSICLDKSDD
     IGLRFLNYLL DLYGSNPSTF PHLNPNSQDK NGNTVMHIIF QKAQTKQVKK IMDLLAKFDI
     NFNLKNKLGK DVRHRIKKND PRLLTWNTAV SEKRKYRQDT VGQLVKLPKS IPVCNTSQPK
     STAHSSSASV WRASPGNSTP ANTEPVPDNW EEADGGQLTK QETGEVNKPL TLREGLVKAI
     TDLIQHLQLG DNPIEDNSQV PNPSSALTSV EGKKSEPQQT CGYESLAHSK GDGADSEKVE
     DTEKECDESD MPMPNGIGEE TVEVNGQVQD FDNMTWEIEC TSEMLKKLGS KAVPHYMKKK
     IILAVQQLGN GEWTQGLQKR LKHLKADIQL YEAKLDKGAR MLWELAIDFS PRCSEAAEKI
     IETEQSIHPL EKSGRVYTEI IRIWDIVLDH CKLDRAIGTI CTAYNRGLSC ILRKKLKGIS
     KIKQSSNLKT QKRIPRCYVE DTEAEKTKEH IIPEYFPPAS AVETEYNIMK FHSFSTNMAL
     NIINDMNSAV EYPFRVGELE YAVIDLSPKP MEPIILIGRS GTGKTTCCLY RLWKKFHSYW
     EKAQQAGAPL LVRQVWQRRK FEIESEKSAG EEEDNEKQHN DDSSESIELE SIDDEQDDEG
     EQCSSADDTE LNLLGDCEEE EEHSTEESDN LEHLHQIFVT KNHVLCQEVQ RNFIELSKSS
     KSTSHFQPLE SNVYKLQDVK DENFPLYVTS KQLLLLLDAS MPDPFFLRNE DGSLKRTIVG
     WSTQEDLVIP NWQEEEEESN AEVEYGEDEK AAEAHSREND PRVFVTYDVF ANEMWPKMMK
     GKNSYNPALV WKEIKSFLKG SFEALSCPQG KLTEEEYKKL GRKRSPNFKE DRSEIYRLFC
     IYQQIRSQRG YFDEEDVLYN LSQRLSKLED LPWSIHELYG DEIQDFTQAE LALLMKCIND
     PNAMFLTGDT AQSIMKGVAF RFSDLRSLFH YASKNSVDKK QCGVRKPKRI YQLYQNYRSH
     SGILHLASGV VDLLQHYFPE SFDRLPRDSG LFDGPKPTVL ESCSVSDLAI LLRGNKRKTQ
     PIEFGAHQVI LVANEMVKDK IPEELSLALV LTIYEAKGLE FDDVLLYNFF TDSEAYKEWK
     IISSFTPSSD SLGESKLVIE TPLEKNIATQ SRSPVLNPEM YKMLNGELKQ LYTAITRARV
     NLWIFDENSD KRAPAFKYFI KREFVQVVKI DENKDLDDSM FVKTSTPEEW IAQGEYYAKH
     QCWKVAAKCY QKGGAIEKEK LALAHDAVLN VQSKKSSPKE KQMDYMYLAK TYLECGEPKL
     SLKCLIYAKE FQLCAALYEK LGKIKDAAYF YKRSQCYRDA SRCYEQIQEF DLALKMCCHE
     ELYEEAAILV ERYEEILRTK RQPVSKLSYS ANQFYLEASA KYLRENKTKE MMAVLSRLDT
     EDQLVFLKSR KCLAQAADLL RREGRQEEAA MLMKQHGFVL EAAKLTTKKE FRASCLLAAV
     RFSVTGCSEL ENRDTILEEA LELCKQTNQK SSIAEATFLQ GVLKKDFRKL EEAFYKFLPL
     NHCAGVVEAL FESTHCEPKS QGIFFLAPCG LEALLNLFRA LQKATTNAEK EMVKSCFDYF
     GILPIDGNVC QVSQNEAGHI LQFLPDSPVL KEKKTKDHFI VGMEEVKSAL NKHFLSRLCS
     ITCSILEQSY PDICMKFIAG LKCEDKTCKD FHRPLLRHEA KSILQCKMHL AAINGLLLQA
     KRLFPKELLH EFNDIDEILT ADKYILCKSL LDFVFPKHFH LRVVSENPKA CKDILGLHQF
     SKPCRMVLKE YIIFQFKSEN AINRRESTDL WLRAMQVFIL SSSYPEEFEK LLAKEEDDYN
     KELKLLEAKK YEKEERGRGG RPKGVDGRYG MLIPDKYSGN AENTHLCFIR LLENSLERLY
     VYRNPEDCKW MFFRFMNVLV KKCIEPLIPS IGNTVMLLEF QYILCCAVLM RLCKNITLCL
     PKSYIALFHY WEFLFRKKDP KKEIRDMFSI IQEYKPKDPN EAVKEFKFHL LYVAKVLCGA
     KNSNFNVLLD AFRDPDCITS GEAERTMVLC LVMLVNADQV LSPRCKSLLH EHFPEIKSKL
     INMKKDCPSK VPERLVKIVE RVNDAVDMRK IAEGLQELLI ERDEEYLADC HWKWDTMYAK
     GASVRGIFYE QVNLDRFESH LDPLEYFEEP ETELERDLYV EEREDPLTAI ASIKQQKQQQ
     KAHAKRKLWR LFLLAYYCIK WRRNSCSKTD PIGMEMKELM SGIFKKADID RTQCDLCGVK
     FIQGPENYFI QKEDLERETS EAVTPTETDP GEKESIERSE TVVASETYVK HRHLDEHRNK
     YTAYQNYFEF FKRNVDPKLR EGLDVVDTIE QNTWITSHLI FKEHSNVVQR KIQENIKKIS
     DIVEDIYKRK AWADAEEIMA KPVSSLSVNL GDARKWLKNT ESHMVKEEEV SSLVLAGSID
     GGNREGYRKM GQISEAKGCS PLEASETIAI KAQDCQGDAG KPIKAKGEGK EVRKAKEEGA
     GGEENVVHGE NELTRMKKMG EHKANKDEKK PQEFESTRLR RNVHTRADVE SCYEIGRTIG
     DGNFAIVKQC RCCNTNENYA MKIVDKSKLK GKEDMMENEI LIIKSLSHPN IVSLIEVYET
     EAEIYLILEY VPGGDLFDAI IESIKFTEHD AALMITDLCE ALVYIHGMNI VHRDLKPENL
     LVQHNADKST TLKLADFGLA KKVTKPIFTV CGTPTYVAPE ILAEKGYGLE VDMWATGVIL
     YILLCGFPPF RSQERDQEEL FQIIQLGHYE FLSPYWDSIS GAAKDLITRL LVIDPLKRYT
     AQQVLQHPWI RTAGKTNSRN LQREVTINIE RHFRSQRRKG VVDDNT
//
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