ID A0A165GAL8_EXIGL Unreviewed; 1180 AA.
AC A0A165GAL8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pkinase-domain-containing protein {ECO:0000313|EMBL:KZV90232.1};
GN ORFNames=EXIGLDRAFT_750733 {ECO:0000313|EMBL:KZV90232.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90232.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV90232.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90232.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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; KV426053; KZV90232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GAL8; -.
DR STRING; 1314781.A0A165GAL8; -.
DR InParanoid; A0A165GAL8; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0000165; P:MAPK cascade; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09534; SAM_Ste11_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KZV90232.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transferase {ECO:0000313|EMBL:KZV90232.1}.
FT DOMAIN 73..136
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 900..1162
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..826
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..886
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 929
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1180 AA; 127611 MW; 707AF092F6E6B92B CRC64;
MAAVANGFLH NPPSGRSSTS SSPTSPSFHS AHAAIQRLVP GRPSTPASGA QVAGTVQLEP
PPGLSYLDFV RQWSDAHVAL WLQGCKCGHQ ADIFSENDIR GDVVLDLDHA TLKEMGIVSV
GERARIVNAV KQLRTKCHAS KLITPGPPRV TLTNSNQAPA QDVVFPEAGL ARSNSKRGAG
GARPPPLTLK PSARSDVELV RTSGNTPRPA VSTPSTANHT PVQTSRPFLP PLPPVPRTNP
PPPPSSNRST SSQTQQQRPS NLGLPSQPAP GRARTPTPEP GPPPAYTTQP LPPAPTPTPA
TPSHGWSRDG GYGLPPNPGA YRTSSPHQAS SQPRPSQQQR PAGAPGHQKT SSLSRSAAAA
GHPYAMPTLE PPSFKANDLS PIAESFMSPS GRTPSTLAPP SSVLGRPTTP LNQSNPGIDE
LRRKTLKVYL EDGGSNNYRI INVHDCERGI DVLERVLKKF TKYLDGDQDI TTEGGLVLDG
YGAFYDDSIS DGKPLTDTQL LYVTHADPDS PERELGLRLR LVQQQRYDRY AGEHLRTSSS
QTSLQTSAEI KKMNRASSIS ILSSLGVPNP ERTLLSADTS ASPTRSPGSP TRTNKPGKLR
NFFGQRPPSE LITTHLAEFF PYTEPKVLER THRHSMLRQS TISSKRDSRF RRDSSSTTWL
PPPSSRFSTS TLGSRSRASM ETMPRGSSPP PLPEKPSPAH SPDAGYGSPS RMSFRTGDGE
MVDVKVEEVA DEPSSQQLLP PVPISEPLAF PSLDRRASTA SRMSYLSELR AKRDTSDTAS
MLTVDEITQE VESRRASWIG QSSSAGEETE EEDDEEEEEE AASEEATLLD EAVAGPSGGA
SFRRKPSVGL TGGAKPPAPP ALQVDDEDDD EDEDEDDDDE EETVEGGEMS AAPGQNIAKW
IRGALIGSGS FGSVYLGMNK FTGMLMAVKQ VELPSGSSHN EERKKSMLTA LEREIDLLKD
LQHENIVQYL DSSMDDQYLN IFLEYVPGGS VAALLNNYGA FEEALVRNFV RQILQGLNYL
HEREIIHRDI KGANILVDNK GGIKISDFGI SKKVADNILK NSNRPSLQGS VFWMAPEVVK
QTSYTRKADI WSLGCLVVEM FTGQHPYPKL NQMQAIFKIG QSAKPATPDD ISSDAEDFLN
QTFEIDYQAR PSAAELLTHS WIINDPANPA GKKAAKDAST
//
