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Database: UniProt
Entry: C5FWZ9_ARTOC
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Original site: C5FWZ9_ARTOC 
ID   C5FWZ9_ARTOC            Unreviewed;       361 AA.
AC   C5FWZ9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000256|ARBA:ARBA00018572};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=Serine/threonine-protein kinase atg1 {ECO:0000256|ARBA:ARBA00019599};
GN   ORFNames=MCYG_07658 {ECO:0000313|EMBL:EEQ34839.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ34839.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR   EMBL; DS995707; EEQ34839.1; -; Genomic_DNA.
DR   RefSeq; XP_002843875.1; XM_002843829.1.
DR   AlphaFoldDB; C5FWZ9; -.
DR   STRING; 554155.C5FWZ9; -.
DR   GeneID; 9230846; -.
DR   VEuPathDB; FungiDB:MCYG_07658; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_31_1_1; -.
DR   OMA; LMEPWAI; -.
DR   OrthoDB; 2133671at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0010506; P:regulation of autophagy; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EEQ34839.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:EEQ34839.1}.
FT   DOMAIN          4..361
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   361 AA;  41912 MW;  6E0C2D72D8075F96 CRC64;
     MIPIRKKDCV GCGAKANVHK ASETIVVKVS NSSAPTEDPF LQEVKFYKRL FEEKDRCLDI
     VDCFIALPNY IFLSYCCNDN LARRFFKYQE REIRPNGRPG KLLGIKNIRT LRLFLNGYNN
     SPQPFLGIKV YEDPTLIARW IQQLSSALAF MEKLGYTHND LHPRNCLLDE NLNLKLSDFD
     QTTTIGQFLE SLMEPWAIKL SSGPLSNTYG LTSARTEQFA VGTFLYTMVY GHEPYEDIHL
     EEDPIELRRR FRALEFPELN RHDVFDNLIS ACWYNVYPTM ALVAYDFKRK TKDIASSSDY
     KIVDYVKEKN TCIALLQGGL LGPEWALSYQ PTWRRYLHAI VGNFLFIWKR SVNFLGSLFR
     R
//
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