ID A0A177WE39_BATDL Unreviewed; 3139 AA.
AC A0A177WE39;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=BDEG_22024 {ECO:0000313|EMBL:OAJ38056.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ38056.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ38056.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ38056.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ38056.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ38056.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
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DR EMBL; DS022301; OAJ38056.1; -; Genomic_DNA.
DR STRING; 403673.A0A177WE39; -.
DR VEuPathDB; FungiDB:BDEG_22024; -.
DR eggNOG; KOG0606; Eukaryota.
DR Proteomes; UP000077115; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05579; STKc_MAST_like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF1; SERINE_THREONINE-PROTEIN KINASE GREATWALL; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000077115};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2117..2481
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2482..2567
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 3003..3117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2077..2096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2514..2615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2746..2768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2815..2835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2869..2893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2954..2996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1972..2034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2531..2545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2546..2594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2816..2835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2974..2996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3053
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 3139 AA; 339959 MW; 0271C282FE576A8D CRC64;
MDHHNSPEPT SNASNTSSSQ AYVKGKRSSH PKADRRLSPL NPLSALVAPT SSPTSTGTVF
GQTLSNREYS LGNNQSLMPH STTANTNPEQ PCQPAALTLD LPQLHSGGVS TVSPTSPLAG
SVTSSNEAAA KRRLVGSPFF QMRRPLPTTS AASSTLTSSL SAASIPATLH SSESIESSTS
PVSTIATNSI DARTMVGRVH THPLAATLLP KSKSTGIASC PVSGPGIKDN LLKATHQSIS
GFVSSASKNI PTKATARSDT GDSIIETIDS SSSSVTNMHP SISQHSSINS LSQTRLNQPF
QQSTTDLTTN SGLSFKKPML SSSDTMSNSV QSELNSTNQS PLLFQKFSFN QLSSASTSRA
TLLNSLETPL RTSTMPILHS QSLSGPNSAI STKSGAIIFS PFIISSHCET HDPTNMFNAC
EQQDSNSPTP NRPRRILCLS TSLPDMPQWS KARSSGRTQE MTSWLPVQAS QTTPLVASLS
RNETSEVSWR LVSFGRSPRL PASALSETIS PPQPVNSPTV LPASGQPPST TVSFTTLPLN
SNIPASTVYT STGMYMAPPR LRLRTFSSSS QQQQQVASSY TSPNIKTTNK QYLSVHMNEP
RISALPIKGG NSECLDRLSM GFTVSDLHAY TFVIESSRQA KNAHWTRNPI AFWPPWHDVL
QQQDDNTKVL VKSTDVPSSQ HGSLPKLSLQ LPSPRMYSAP LRLAPTLSSS HTSPQLANSS
IQPSQILQNS GSTSANVNSS ATPLGGIRFQ HRPNSPVRHT ARQSSGIINS PVLAPLPVPI
LDQRSPSPMF ILEDDDASDS SASSGTRSSH RPDGSYYSSN NVRTRSRRLR NPLQVSTVTS
LSGFTGGHVS HSESPNRGAP FASVESPDSD IGSWRGVSGG NVINRSLSDG DLSEYLKGYS
ELKYSLQIAK ATCDVEIQKI LHELAEYIEM HITNHANVTA TDSCQFCASE KQRHCDSTDS
NDVATKGPCD CQAILSTLDE LLKQTNFLKR PFPPIPTLID SSAEVISSVP ATKDGNFQTQ
TSLLLKQTDP ITDSAAQVDL YAIHNLFSPN LHKIDDPPLI ASIRDLIGVA EHIIRMDVTS
LMQPGTCRAL MGHIQELQYQ WRLNPEWPLA HLVVRFLIIF ASVARLLEHL EEDTRMWMYA
SGHNTPGSQS KLISSMAKQF RSSHKTNSFK SKVTDRRISV SPSISSVIGV DSSDADVDDE
GQNTDSQNDT DSRRVYSRKP RQKGSRPLIH KVNKHDLQEK WSFGESHAAV DRSQNFNVLL
EIATDGTITY ISPSAHTVFG FEPTLMVGAM IPPFLPIDTK NVFVEASDKC PCEDGFIMEI
SFSAVRCDGR TLQLEAKGML NVDRTTGKKR SIVWVMRPVG LKGEEWEDAL YCSDQATSSL
TEDHRGDDSM SESSFFDQPD NAFHQLKGLS GSNSTVNAAS LMRINSTLQS TSALVESNAP
GHSISTLQSN LSTGSFISTI ETPLSIHDEP IPNINLALCN ICERSIPAII FEEHAELCTV
LHRTEMEVVL ANDQLKNFRA QCMEKVGLLE DEIGDECKEM ADTAQRRTVQ DIISGSTLTS
ATRDFKVDAN SNDRNKARKR GSDGEGDWAS GSDAIEDDDR RTYLQHLAKL VSIGKEIISV
IDETLAIPIP NSENLQTSPG GSVSEDVEGI YSDHSLLDPS HTHKMGQSGQ SLYTGSPTAS
TQLSKLVLSS ALSHLEFDRL LSWSCPADAE FSTPDLPVST LSKGSGLNLD EEARCPVIDN
VVISLAFAIR NIGVDTMSCI HNKVQSILKL RDEMAEYQRC ILREEEVKVE IGIQTGTLSL
EGDQGSVHVS DRDYASSERV ERSLHNSSYG ESSTNLPQSP LRGTQPHLLT SLANFADEVM
GSPRQSICSS PVTTISPSAI LYQLTANKGS GSNISHLSSN GSVNKLTLPA HHPHNLDRKF
GFPAAPPFIR SGHNEGNGSS TNLNEATVQE PDHNTSQTKP ELNPMSAPRS KLKRNKLTSS
LNIRTTSSPE GNDQGFQKSN KNSQRHLRAS SGCADQQGDE PVSQPSSRSP SVSQFLQRGI
ASPIISQGTH FTPVSTSTCS AAPSQLTNSS LFFGSQSNGV SPPSSVPTSP MVTSTPLSST
CLTPSISQRA IPSIKDYEII KPISKGAFGS VYLAKKRVTG DYFAIKAIKK ADMVAKNQVM
NIKSERMILT QLDSPYVVKL YYSFQSKEHI YLVMEFLNGG DCAALLKNMG QLDETWAKQY
ISEVVLGLEF LHSRDIIHRD LKPDNLLIDS NGHIKLTDFG LSRVGFLGRR ARGVGDAVGG
TLLVDRPFSA LSPGHPLVSP IGPSGFTLPS SPLPKDHPLN FALHPQTQHL RGGGSGGSSG
LPTNLHSRRG SMASILGATD SGPVLGGRLA EKVDEKDSKQ FVGTPDYLAP ESILGLGQGA
SVDWWALGVI LYEFLYGIPP FNAKMPSQVF ENILTRRIVW HEDDIEMSDT VRDLMEKLMC
SDIHARLGTE GAAEVRSHKW FDHVDWDNLR LNKANFVPKI SNIEDTDYFD DRGVATNMSD
GSPKQADGPL SAKDKQTKDT HHTPDQQHAS SFLGISGTDM LTESSSGSTT VKFGPVGSSN
RSATEAVINS FNDDDDANKS SEDEDEEYLK SASADGEAPD FGEVVYKNLE LLEKANKQLV
SRIRSDFPEG EEWKQRRRES LPLSTPPIGV FRGTGVSSFG YTLTGVSPSS SLGSGNVNVN
QGFFPSPPTR LRTLSANATG LPSSGNFVTS RPTTPTNLSS MLSIEKNSQD ELNESAPRPS
AHPVNDHNVR HADTSAAVSK QMQTVISESG MRARRSSLPS FPTRFRVHTQ SPEFGFARPH
VTSNTPSSTP TSGGVPTFTS IPNSATLTSS GLSKVGQNAH CEPAIREVAG RDQSLKPEHH
GSTRLSTTST SSYQSYLENA KQQLFREQRR GSSFSTHSRE ASILTSSLTG PESLIEITSP
VLPLSQLSRP HFLSEHTHTP QHQPLHSSAK DHRRSASSAG SSNTPSSISS HHSQNSPIGR
QLDALIACDN VAETKELESL LAGQHCRCVT VRSGSEILQC AMGDARFDII FLDTSMPQLN
GESVVRMIRS TKNINQHTLV IGIISGQPTF LQSQQFDDTL SKPFSKEILH RILVAIAPSD
SMLYYEASGN LYGLPNNKI
//
