ID A0A0E1S2Q0_COCIM Unreviewed; 1578 AA.
AC A0A0E1S2Q0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=TKL protein kinase {ECO:0000313|EMBL:EAS32262.2};
GN ORFNames=CIMG_03286 {ECO:0000313|EMBL:EAS32262.2};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS32262.2, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the fem-1 family.
CC {ECO:0000256|ARBA:ARBA00038500}.
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DR EMBL; GG704916; EAS32262.2; -; Genomic_DNA.
DR RefSeq; XP_001243845.2; XM_001243844.2.
DR GeneID; 4564771; -.
DR KEGG; cim:CIMG_03286; -.
DR VEuPathDB; FungiDB:CIMG_03286; -.
DR InParanoid; A0A0E1S2Q0; -.
DR OMA; TRHEYET; -.
DR OrthoDB; 2419497at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR24173; ANKYRIN REPEAT CONTAINING; 1.
DR PANTHER; PTHR24173:SF74; UVEAL AUTOANTIGEN WITH COILED-COIL DOMAINS AND ANKYRIN REPEATS; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:EAS32262.2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transferase {ECO:0000313|EMBL:EAS32262.2};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 58..387
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 793..825
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 967..1000
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1079..1111
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1345..1390
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
SQ SEQUENCE 1578 AA; 177375 MW; 3220A58B21B55DCE CRC64;
MDSSSSAFSR LSLGDILTPQ TTRPTDKSLA GDTDIFQIDR FISESFDSGL LILDENEFER
GEFLGSGRSM STYKGKWKSR SRPVALKYIN LSPPVGTSSA AARGTELQSI LRSAALELRV
LQHETTRIHP NIVEILAVSW QQITTLTGQC EIYPILIMEL ACPDYPTLGE LAKKEFHNLS
LTIRLSLLRD VFEGIAVLHE LDIVHGDLKP DNVLIFRDAS GNLTAKISDF GFSQVELPAG
SPSFGAGGTE YWNAPECLRD APDPLAIFRK EKSRDFYSYA LLAVSIFLGE PPFDKQGWNL
AEISRMKLQD EISGQFASRW RFIESRFKQD PTQWRNLSGP LLWEVLRKDG WSPEEDLPLS
LLRLIPKMLQ LEPSKRPTTH EIRSAFRLCT GDRVIKPKVN RVKNDKHVIF AGGAASVMGN
RSTRAHSLCN PAIPHNLRFA LFKSFLVSAR DQNQARRTNA MVNIGYCMIN AFGTRFDLPE
AIVWFGRAGM EGDTTGQEMV FRLERVLKKS ATELVLGLNN STRVNWMVTC LLRDLGAPQL
PNILPPEIHL ERPQDKLKDI LLGFEPELVE SGLRRAVDDA IIKTLAPQSK DYSKDPAWKS
FPGLWDAVVS DDPAAVSELL DVNDPRWTPN VRETFILTAL EQRAMNVLRS LVYEHKFYID
KVFEIALGRA FLKSDTEMIA LLLALEVPWD IMFGSNSLNS VLTGCTVTTI TVALRLFSYL
KVDDSTEYSP YWDEGVLRRE IMDGIQPGMC SLPSDVGTVD NYAPPIFETI VYNRPLNLWL
ILSLGGNPNV RYMGMTALHF AVKMLRPLLV AMLLAFDADP NTRDTRHEYE TPLHQISRQH
MRPLNTPRDT YFQALDVFGD KFVPAPEYPD EDNNHRRLII RLLVEYGADL NALCAEGMTP
LTKAVLSQLP HAPIIAKYLI ELGADSSIAG ASGFSSLHAA STKGSLQLLR YILYLPGLSM
LNLRSNNGTT PLMAASTDDD RAHHLIELLE AGADIGLRNN SGHNALSIAM KHSRKIIFDI
LVTHITQVPP RLREAVFVNA VSGITAAHDA FASKDQEMIP HFLRRMIPIM THFHRPNKSG
LTPLHLAVLK KHTAALRLLL DNGANVDAKT DKGMTPLDLA RGLRERTFVN ILLRWKGESQ
MRNEPPLAPE QFQSLSAASA QYADEVASMH GEGNGSTSQS AETDLQAARY KQKLMNDSQY
IPNDRFTRDT ADPSKGITKI EEVHSKMLEI SVSRKGEQDY TSLWRMNNLG CVYERFGRLF
NAETIYRKGW NISLEVLGNN HILTADFANK LVRVLEDLGR PEDPVLTEWI SWYGKDTLEP
PLFQLRSQPG NAYSGSTSST RPEVEEICAR LECNNSSRLT CQKCLVYRFC SESCRSLEWE
DKTSSHSREC IHSLTSEETP AIVSQKLVPE DPYAQKLTSF IYSRIMAGFI ESDFGERPPT
VYSAHLILYD PKAFHTPVRF RTKKNTAVMF LSNGGFQYLF KATDSQWKTP RRADMMLLYT
EVDFWVSPPR ESMPQQSPAA AAAADGTTAN TEMLLLVDYI YLDFPKAQER RQQRLSSVNT
DIRVIQCDYA GQKQKMTN
//
