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Database: UniProt
Entry: F2TXQ5_SALR5
LinkDB: F2TXQ5_SALR5
Original site: F2TXQ5_SALR5 
ID   F2TXQ5_SALR5            Unreviewed;      1450 AA.
AC   F2TXQ5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=TKL protein kinase {ECO:0000313|EMBL:EGD76164.1};
GN   ORFNames=PTSG_00871 {ECO:0000313|EMBL:EGD76164.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL832956; EGD76164.1; -; Genomic_DNA.
DR   RefSeq; XP_004998339.1; XM_004998282.1.
DR   STRING; 946362.F2TXQ5; -.
DR   EnsemblProtists; EGD76164; EGD76164; PTSG_00871.
DR   GeneID; 16078934; -.
DR   KEGG; sre:PTSG_00871; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0197; Eukaryota.
DR   eggNOG; KOG0379; Eukaryota.
DR   InParanoid; F2TXQ5; -.
DR   OrthoDB; 5018984at2759; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   PANTHER; PTHR44329:SF313; MIXED LINEAGE KINASE DOMAIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 1.
DR   Pfam; PF13415; Kelch_3; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   SMART; SM01411; Ephrin_rec_like; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF117281; Kelch motif; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:EGD76164.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   Transferase {ECO:0000313|EMBL:EGD76164.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        950..972
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1014..1445
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          542..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..580
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  160446 MW;  2C240159EC0A1ED7 CRC64;
     MAVDTPVPLK PATQRRTATA TTAMGIAAAV VAVLGIAISV VPCELAHARV IIPYNAPELV
     TSKTATPPSL AWHTTTLLAL ESDFISVTVG GGNANDIANN RATIRLSDDI WVFSRKLNLW
     SVCEIYSGAA NASDPRFRTR MHHAAERITP LSVYNTSSPA RRPLREGAGK LMVLGGAVYI
     DNNVTILDDH WMLEVWRSPI ETQSFFTCAW TRLEKPAAMA PRFLPAVSAA YHPFELYSFG
     GCLEARRRHI DVGDTTEIFL ECTDTTNEVW RYTEDLGWSL LAQAVPADSA SLLRPLLSSL
     MYRVGGRVPR TYMIYGGFPG RASPYVANVS MCTFPDPHAA TGSTTFSCQA LGSACVFNQY
     RECKDEVRFV SRGAVIPLGN NRTVLFGVPD GISDSLVGFL HEYSTDEPAP RFTEIRSLSR
     LLTPVFSGAS SRIGLLGGFS ATPLAAGIDV EQFLFFGDFF RPQTGDAWST WLYTPQSLTA
     HSHAPVLSGV WQDKFFYSSM TARAWPSSQT VGHWVIQLGG YTGSVANSDW KFDVGGVLEA
     ERKEREKQQQ EEDKAKGESM EDDDDHDHDD DDEEEPVNPE DVVVFDEENV DAEALTVWVR
     LDELDQHTSP FSRFYGSSAT VNDSAMFVFG GQRKPRSGCA NDAFFFFPET HRVVVQEGGP
     RPAERRGSTL VRMGSSIYLY GGEDCDNEFF LDDLWRFDLH LMRWFQLSRA ATAPIASSYH
     TAAALKTSEN VTEMAVFGGF RPRNEYDHFG WAFNPQTQAW RPIESDEEPL WRTSHCAVRM
     DEGPIAGQLV MIGGASRLGV DLGDGWLYHH ASQRWQRLRD NHVRFSLSPG RLGHTCSAFR
     DTVFVFGGTS RQRFFRSVIA FRPTCNPGFS ADNGQCVPCP LRTYRSDLSN PSCVQCSGDL
     TTKTEGATDV SLCNICRDSA CVHGTGTAVA SDCICRCSFG YSGKACDINV LGIVLGTLFA
     LAVIGFATWH VLRFYRRVAT SIKQHSALQQ RLLDEKEQEI ELFEQIWTIS PDELQFVRVL
     DEGAFGRVEL MVWLSAGLNV AVKRLREAIL QLDDTCKQDF EREVKFVRQL RHPNIVRFHG
     AYLGAQPFLV MEYVERGSLQ TILADNAVPI SDARKHSFLC DTAAGMHYLH QKGRMHRDLK
     SANLLVTMDW RIKVTDFTTA KNVVQDALTR QRRASQVSAG MAHARNATMS ALGRQHVEGT
     RGGGQGGCSW LDADKKASTM GKVCGGLERT ACKFTRGMRR RGQAKSMSVL PRSDGGDKFD
     FDELPVSLQA QAQHERRDTG QQLLVADLDD GDGNDETTTD SGGGLEGAML LTTDSDDEDA
     VVIGERPSPA ATQRNEADYA NIWNQTTGIG TIPWTAPEAL ADKAYGLPAD VYSYGIVISE
     ITTRRLPYWD YKGSIRKGVL AGLRPTMPED CCDRRYIDLA AQCWCENPQE RLTFSQIVTT
     LQSFDGESSL
//
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