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TBCK_CHICK
ID   TBCK_CHICK              Reviewed;         893 AA.
AC   Q5F361;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=TBC domain-containing protein kinase-like protein;
GN   Name=TBCK {ECO:0000250|UniProtKB:Q8TEA7}; ORFNames=RCJMB04_32m11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000312|EMBL:CAH65423.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAH65423.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAH65423.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Involved in the modulation of mTOR signaling and expression
CC       of mTOR complex components. Involved in the regulation of cell
CC       proliferation and growth. Involved in the control of actin-cytoskeleton
CC       organization. {ECO:0000250|UniProtKB:Q8TEA7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TEA7}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8TEA7}.
CC       Midbody {ECO:0000250|UniProtKB:Q8TEA7}. Note=Mainly localized in the
CC       cytoplasm during interphase. During metaphase, TBCK accumulates at the
CC       mitotic spindle. At the end of mitosis, it is detected at the midbody.
CC       {ECO:0000250|UniProtKB:Q8TEA7}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH65423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ851789; CAH65423.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001012595.1; NM_001012577.1.
DR   AlphaFoldDB; Q5F361; -.
DR   SMR; Q5F361; -.
DR   STRING; 9031.ENSGALP00000017170; -.
DR   PaxDb; Q5F361; -.
DR   GeneID; 422534; -.
DR   KEGG; gga:422534; -.
DR   CTD; 93627; -.
DR   VEuPathDB; HostDB:geneid_422534; -.
DR   eggNOG; KOG1093; Eukaryota.
DR   InParanoid; Q5F361; -.
DR   PhylomeDB; Q5F361; -.
DR   PRO; PR:Q5F361; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR   InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00566; RabGAP-TBC; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; SSF47923; 2.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..893
FT                   /note="TBC domain-containing protein kinase-like protein"
FT                   /id="PRO_0000273280"
FT   DOMAIN          1..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          466..651
FT                   /note="Rab-GAP TBC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT   DOMAIN          790..889
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ   SEQUENCE   893 AA;  100453 MW;  E40C85C13AF6EC62 CRC64;
     MFPLRDTEMG ASTFFASALP HDVCGSNGLP LTPNSIKILG RFQILKTITH PRLCQYVDIT
     RGKHERLVVA AEHCENSLED LLREGKLVSS SRILCIAYEV LQGLQYMNKH GMVHRALSPR
     NILLDRKGHV KLAKFGLYHM TAQGVDVDFP IGYPSYLAPE VIAQGMVKPS DHTQCEKPLP
     SGPKSDLWSL GIILFELCVG RKLFQTLEIA ERLKFVITLG YVDDIVTVLA EEHGCLDIIK
     DLSENVITLL KKCLTFQPSK RPTPEELMHD HLFSEVSLTY PPFHKPAGLF SSSPRCADLT
     LPEDISQLCK DEDNDYLAER SIEEVYYLWC LAGGDLEKEL VNKEIIRSKP PVCTLPNFVL
     EDGESFGQGR DRSSLLDDTT VTLSLCQLRN RLKDVGGEAF YPLLEDDQST LPHSNSSSEL
     SAAANLPLII RERDTEYQLN RIVLFDRLLK AYPYKKNQIW KEARVDIPPL LRGITWAALL
     GVEGAIQAKY DAIDKDTPIP TDRQIEVDIP RCHQYDELLS SPEGHAKFRR VLKAWVVSHP
     DLVYWQGLDS LCAPFLYLNF NNEALAYACM SAFIPKYLYN FFLKDNSHVI QEYLTVFSQM
     IAFHDPELSN HLNEIGFIPD LYAIPWFLTM FTHVFPLHKI FHLWDTLLLG NSSFPFCIGV
     AILQQLRDRL LANGFNECIL LFSDLPEIDI ERCVRESINL FRWTPKSATY RQYAQPPRQA
     NESNGTRSSM SCFSVDYQEA PRGDLSRDSI KLDDLKAEVS PRISAEDLID LCELTGPSHS
     KTPIKKTKSS KPKLLVVDIR NSEDFNRGHI SGSINVPFAS AFTAEGDLIQ CPATATLQSF
     KGRVVVIVGN AVKNTAAFAA HLVKSKYPRV CILDGGINKI KPTGLLTVPS PQI
 
 
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