ID A0A1S8W030_9FUNG Unreviewed; 1589 AA.
AC A0A1S8W030;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BSLG_03169 {ECO:0000313|EMBL:OON07343.1};
OS Batrachochytrium salamandrivorans.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON07343.1, ECO:0000313|Proteomes:UP000189906};
RN [1] {ECO:0000313|EMBL:OON07343.1, ECO:0000313|Proteomes:UP000189906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS {ECO:0000313|EMBL:OON07343.1,
RC ECO:0000313|Proteomes:UP000189906};
RA Lavstsen T., Jespersen J.S.;
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=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OON07343.1}.
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DR EMBL; LYON01000415; OON07343.1; -; Genomic_DNA.
DR STRING; 1357716.A0A1S8W030; -.
DR VEuPathDB; FungiDB:BSLG_03169; -.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000189906; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20826; C1_TNS2-like; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988:SF71; CITRON RHO-INTERACTING KINASE; 1.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF46585; HR1 repeat; 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; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 104..369
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 370..440
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1452..1502
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1104..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 484..605
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 662..724
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 810..981
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1010..1075
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1363..1390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1104..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1589 AA; 180595 MW; 2B116A802EB19796 CRC64;
MALTPSDFST SIQGRLEQLS QYISTENNQP SLSLEVLLDA FLAVYIDCKS ASKTNDQISG
FIRQCKQTGL PLLLLRAKKD LWDEPFSLPQ YHRPLILRVN TRDFEIIKTL ATGAVGRVCL
VRAKKDAMVY AMKILKKSDL LTRSEAAFFM EERNALVFSE KSSWITTLYA AFQDEDNLYL
VMEYVSGGSL RSLLNNRETS MEEKEARFYV AEMILALEVL HKYNYIHRDV KPENCLIDSS
GHIKLADFGS CIRVNETSRV TSHETVGTPD YISPEILRAH EGNANYDQSV DWWSLGVILY
ELLFDEVPFY SESLVETYGK IMDHKKHFAF PDDIEISDVC KSFIQGLICS ADVRLGRNGI
GDIKNHPWFE GICWETIHES TAPFVPELSG PEDTRYFEDE ENESKKFAKK PLDRNREFSG
QNLAFVGYTY VKNATAQILW PGMGDQGIAT NTVNLMVGQD QTTGFSRANS AANTAAYSII
KEQLDTETQK VLSLSADKKQ AEDEAANLKA SLNRESAQRL EMQALVSTLE KERNKLESEF
KQLKLAQDRD HHNRSELEEK VTQLKESLNK EVKNSVETQE LSEIRIRLEK EIGTLTAMLK
DEKAQAVKRE IGILELSKAK TMLDKETAKL SDALKLERQL KQDAIGQSDE LNQKVVAGEK
TISTLESEIK ECELNVSRQI KEIASLKSTL KADSEKLLLA SARTAELEKK NALLLIEVDS
LQAKLGEARV REDELIATAR DQQSTRSETA SHEIDGLRSQ LSVQVAARTK VTDELAQLSK
AKALIEMEYA DTKAKYSTEV QLHQETQKSL SLLQETAEES SRQISALENS SRKAQAQNGV
AVFNSAALAA QVSLLQKQIE ALEETNSGLH VENDTVRTEL GIMSLELQNS HHANDKLQAK
IAELEATCSA ELKARINIES LRANLHKENA QLLQESERFR SRIDVITHEH ENTISEHHGA
IVQLRSEFKE LEEKLTMERE QRFQMEYSQT MMTRKTQELE ENGKRETALR MQAEKSLDSA
NKRVRELGSE LETELEREQQ LHQRINDLET VSDALKCKLE MADELMRERD REKDQLLVID
TKNRVEEKTP TRFKIRGMFF KGSRDSTEIT PDRSVQKLQD PEEDGRNNKD ADHRRKQSHQ
SMDSLASSLK LQLPLNSKIP ELTTQDLFNP GDVLRGWLKI PKGGKVKKGW KLQFAIVREL
KIYIYEREQD VDSLPGTQII DIMSDIFLAK AVSQNEVIHA NGRDIDLIFK IQAWTSGGTM
SEESETYEIQ QRVQKLQIDI ELEVKMQKAA EKILSVTTDA QKVTVISQMD SSNKRLRALK
AELEKLTPIV SRSIDQANES LSSSKESLEN GSLVAESISS KCMDECQSLR KELEAQLEDE
TKKRDALHKL AYSDHRKKQK DVKDVEVELL TTDRVIAKIK ESLETLSSGD REKTDSLLQR
MRKLSKTTDL MGHFFTSRQY YKPTDCSMCH EALWDTKNQG LECTACKMIC HKTCKPHIDT
SCQDIIKLQS VAPMYFLAKD IQDRARWLVG LTYLRKEYEL SHRPHDGATS TPEKRMSSFM
EQVNSKRMSG IFSAQGTLTS RKDTIKERS
//
