ID G4U737_NEUT9 Unreviewed; 961 AA.
AC G4U737;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Serine/threonine-protein kinase sck1 {ECO:0000313|EMBL:EGZ77439.1};
GN ORFNames=NEUTE2DRAFT_162235 {ECO:0000313|EMBL:EGZ77439.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ77439.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ77439.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL890999; EGZ77439.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U737; -.
DR STRING; 510952.G4U737; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_0_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05586; STKc_Sck1_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGZ77439.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 350..528
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 556..817
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 818..901
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 961 AA; 104937 MW; B55E832BE869E52E CRC64;
MSGPAESAAG QTAPASHSAG SHGHGHGHGH GHGHGHGHGH GAGGFDLLKR ATQAMMSSRP
AATEEDGSDQ IGLDSPRSGV ATPQPDLHDK RLPGIMSYFN QVRSQSSFSR FLPFKANEQT
TAASEAVAPQ TEEPLRASLT PRLPLSAVEQ ETHSVSGDEG SLLLAHEALG PVADVTPPAD
DQMHPYPTPP TSQRSSVRNF KGDAGSEKPR DATPPPSSRP ASLHQMNVPD GGRGIGVARR
SSLLALLTAT VDGLSVPAPH LSNPASPAPN VPNSTSWLRG SSGEPEDLSY PSPSVAHLTK
LTDVTATKSG ASTPTRALST TQPSQSEEKQ PEETSRTNSE GSTERDNRTA SQTPTPSTSS
GGAPASRGKL TIKVGEARGL RRCRDPYVVV VFQRSELISP GPRRAAENDD DAAIAAVQTG
GIPIQRQSSD SGRPMAIPMR SRQSSNTSLT DFNTFRRRNS SQSRRSFTNP TWDAEAVFDV
VDSDMLVDIS VYGQGPSGEE FLGHVDFQAN KAEPIRGWFP LQGHADTMAE NAPTGELYVE
AHYQRAEQKH FGPEDFQILR LIGKGTFGQV YQVRKKDTGR IYAMKVLSKK VIVQKKEVAH
TVGERNILVR TAMSDSPFIV GLKFSFQTPS DLYLVTDYMS GGELFWHLQK DGKFEEKRAK
FYIAELILAI QHLHENDIVY RDLKPENILL DANGHIALCD FGLSKANLTK NDTTNTFCGT
TEYLAPEVLL DEAGYTKMVD FWSLGVLVFE MCCGWSPFYA EDTQQMYKNI AFGKVRFPRD
TLSLEGRNFV KGLLNRNPKH RLGATDDAEE LKRHAFFADI DWDALSKKLI TPPFKPQLKS
DTDVSYFDPE FTNALNANGS LNERAAALAR GYATSTPLSP SVQANFQGFT FVDESALEEN
MHDRHYNRYE DDEMDDVADR RRTDDWEDVH GADQRAANRM SGVVKSNTTE DQMFGGTNFD
P
//
