ID A0A074WHX7_9PEZI Unreviewed; 905 AA.
AC A0A074WHX7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=MAP kinase-like protein {ECO:0000313|EMBL:KEQ71229.1};
GN ORFNames=M436DRAFT_50890 {ECO:0000313|EMBL:KEQ71229.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ71229.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ71229.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ71229.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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}.
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DR EMBL; KL584714; KEQ71229.1; -; Genomic_DNA.
DR RefSeq; XP_013425422.1; XM_013569968.1.
DR AlphaFoldDB; A0A074WHX7; -.
DR STRING; 1043004.A0A074WHX7; -.
DR GeneID; 25411336; -.
DR HOGENOM; CLU_003051_1_0_1; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000027730; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; PF14847; Ras_bdg_2; 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:KEQ71229.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Transferase {ECO:0000313|EMBL:KEQ71229.1}.
FT DOMAIN 42..105
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 624..897
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 905 AA; 99787 MW; 0BF4D4750CEE2D9A CRC64;
MGSQAYQNTS PAFRNNNNPV YGSPTESEFS DSSRMSDTVK NWDEQRVAEW LVSINCGQYV
DIFKANNITG ENLMDMDPAT LKEMGVNKIG DRVRIGSQAK LFRTSVYKKT SKRNMNRLSL
ATLDGNAQMN APPASSPRER AILSTTRIQQ PPTSLRDKRL SRRIDGQDLA KANSRPSSPL
IDQENRSRVP MQKSSSTPYL PKPSQRLTPG ETPPRFGGPV AGHIRSSPSV DNLATYSSAL
PADKALIRVI FDSGRSSMIN IEGCETADDI VLKTLKKGAL NENHVKNFCF YLLDGFNPDP
KYCRRLGDTE LLRICNDRVR GERGRLMLRK IHAGEPEGEQ LRIAAKIAEK EAPSPPAIEV
QQPINKSKSH LKIEQLIGEP LAAVSYPMSP ASLLERERNS YFAAQPAINT AGARARKLKE
FYGARPPTEL ITQDLTSYFP DIEKEEMDKT VRMSMRRSRR LSRAANRLST MSSFSIASSL
KDAPPLPTIA DSWLNSANQP KQLRPLSVVR LGRPISNYRD SITSSVLEPL DEESPLEPNR
KSYVSFGADS GSDSTDRNVA VTDPEGNTIM QSYFDDTGST SPANTENGGS LNSRLSQVIA
EDGEESDDEL MEHLENDSWE NLKYMKGAMI GQGSFGTVYL ALHAITGELM ACKQVEMPSS
SGTHLDAKKN NMVEALKREI GLLRELKHPN IVQYLGSNSD DSHLNIFLEY VAGGSVATML
VNYGSLGEPL IANFVRQILS GLAYLHSKDI IHRDIKGANI LVDNHGSVKI SDFGISKRVE
ASSLLVPSTG KRTGPRVSLQ GSVFWMAPEV VKQTAYTRKA DIWSLGCLIV EMFTGVHPHP
NCTQLQAIFK IGSSAAQARP DMPEQASENA KVFLERTFEI EHEKRPSADE LLGYAFCAPK
EPGSA
//
