ID A0A177DPB0_ALTAL Unreviewed; 2096 AA.
AC A0A177DPB0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=CC77DRAFT_1039824 {ECO:0000313|EMBL:OAG21585.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG21585.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG21585.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG21585.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR EMBL; KV441476; OAG21585.1; -; Genomic_DNA.
DR RefSeq; XP_018387006.1; XM_018527173.1.
DR STRING; 5599.A0A177DPB0; -.
DR GeneID; 29112767; -.
DR KEGG; aalt:CC77DRAFT_1039824; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1039824; -.
DR OMA; KAREYTW; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 45..311
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 753..774
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 914..1593
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1651..1841
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1948..2009
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 416..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1488
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1807..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1919..1957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2009..2096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1932..1949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2038
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2051..2069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1007..1014
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2096 AA; 232814 MW; 86F4EE417EB0DC7A CRC64;
MPSTLCDLVL DSIISPTTTT TPMSASSIHA DAPPAVVQDP EGLQYETGAQ LGKGGFAICH
RAKLLGHEHL GSSTVALKIV KSKMEPPKLA QKFVTELQIH SKLSHPNIVE FFRAFSFESS
TYVVLELCEN GSLADAIKKR KYFTMPEIRR FMIQTCGAIK YLHQRNIVHR DLKTGNLFLD
RDMNVKVGDF GLAALLVSQS DYGAIRRTTM CGTPNYLAPE VLEKTGKGHD EKVDLWAIGI
MMYTLAVGRA PFHAAKREDI YRKLKAREYT WPDLARFANE ITDDLRDIVS LLLVHEDERP
TPDQIVAHPF FKLGYIPLEL DSGCTSRVPK WPKNRPPTAS TIRRGYTEEW WQLCKSSSVG
EYEQGKAFGT YGRRTNKTVA RDCQKEIEAG KQPNIPFSKD VVYVPFPARV QWPHLPTGGL
SEISEEKESS LESQALSETT GNERTKSRVA RAPRREQQAM QTLKENVEPV QEPEPAHRIL
DKQPTRLRAA RKISNPGRVT ANTASAPAPL RVPREARTST RARTAKESAK EAPKTTSNGL
PDLPPLRVTK TSVEESDKPE SAAQATSTKS AARYRTVSND MPATDPVTVL ARLMTFRDNL
ERALDKKPTK SRRDQPPQLP FVAKWVDYSR RYGVGYVLND GSIGTLLSAE EQYPVTIAFA
TDGYNHLRKA GGNRELAKSV ALNYYTTVKK DRGLSQIEVL ESRRVEEIRT VWHKFGKYMC
ATFGDEEKPL RKDPRVNFVR FYQRLGNVGI WGFDDGSFQF NFPDHTKLVL SSDAGYGHFL
CLPLDATSLL EETGNVPWKH VKARAHLRGS LQQLLYGSAD KEDSYKELTE GNLLRAKIEF
IYAVVSEWCQ EGGLGCLVDP KVYSWGGPQL EESKRLDWAS GKTNRAARKA GGGAQPKAQF
ATKAVFETTK KKEVGVSDLT LISKVSNEAI NENLKKRFEN GEIYTYIGHV LVSVNPFRDL
GIYTDQVLES YKGKNRLEVP PHVFAIAESA YYNMNAYKEN QCVIISGESG AGKTEAAKRL
MQYIANVSGG SNSSIQEIKD MVLATNPLLE SFGNAKTLRN NNSSRFGKYL EIHFNAQGEP
VGANINNYLL EKTRVTGQIT NERNFHIFYQ FTKAASSQYR EIFGLQQPQA YLYTSKSKCF
DVPGIDDHAE FDDTLNAMKV IGLPQAEQDN IFRMLAAILW LGNVTFREDD SGNAAIVDQS
VVDFVAYLLE VDSAHVNKAL TIRVMETSRG GRRGSVYDVP LNCAQAGAVR DALSKGIYFN
LFDWIVERVN VSLKARGATA QSIGILDIYG FEIFEKNSFE QLCINYVNEK LQQIFIQLTL
KAEQEEYERE QIKWTPIKYF DNKIVCDLIE EKRPPGVFAA LNDACATAHA DPTAADQTFV
QRLNALSSNP NFTPRQGQFV IKHYAGEVSY AIDGMTDKNK DQLLKDLLNL LGQSSNTFVH
TLFPNQVDQD NRRRPPTAGD KIKASANDLV TTLMQARPSY IRTIKPNENK SPKEFTDANV
LHQVKYLGLQ ENVRIRRAGF ASRQTFDKFV ERFFLLSPKC SYAGEYTWTG DYETGAKQIL
KDTNIPAEEF QIGTTKVFIK TPETLFALET MRDKYWHNMA IRIQRAWRNY LRYRTECAVR
IQRFWRKLNG GKEFIEWRDQ GHKILQGRKE RRRYSLIGSR RFMGDYLGIG NKGGPGEVIA
GAIGISSNEE VPFSCRAEVL VSKLGRSSKP EARSLILTKK NVYLVKQVMV NRQVQIQAER
TIPVGAIKMI SCSTLKDDWF SIGAGSPTEP DPLVNCVFKT EFFTQLTNVL RGSLTLQIGE
TIQYNKKPGK PAQVKVVKDP AVPRDDLYKS GTIHTGPGEP PNSVSKPTPK GKQIAAKPIT
KGKLLRPGGP GGGPSKLASR PAQPRAVPTP AAAQPRAVPQ PEVSQARPVP APVAALSNGM
GAHARTASAG SSRTPPPPPP PPPAPAQPKE PRYKALYDFA GQSAGELSLG KDEIILVTQK
EGNGWWLASR LDKSASGWAP SAYLEEVVQR AAAPPPPPAP PARPANGKPK PPAPPAKRPA
ARKAINGDSG RDSGYSGSGG STMESARDSS GSIAGGLAEA LRQRQAAMHG RKQEDW
//
