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Database: UniProt
Entry: C5MC45_CANTT
LinkDB: C5MC45_CANTT
Original site: C5MC45_CANTT 
ID   C5MC45_CANTT            Unreviewed;       688 AA.
AC   C5MC45;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Association with the SNF1 complex (ASC) domain-containing protein {ECO:0000259|SMART:SM01010};
GN   ORFNames=CTRG_03637 {ECO:0000313|EMBL:EER33212.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER33212.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER33212.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000256|ARBA:ARBA00010926}.
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DR   EMBL; GG692398; EER33212.1; -; Genomic_DNA.
DR   RefSeq; XP_002549340.1; XM_002549294.1.
DR   AlphaFoldDB; C5MC45; -.
DR   STRING; 294747.C5MC45; -.
DR   EnsemblFungi; CTRG_03637-t43_1; CTRG_03637-t43_1-p1; CTRG_03637.
DR   GeneID; 8297771; -.
DR   KEGG; ctp:CTRG_03637; -.
DR   VEuPathDB; FungiDB:CTRG_03637; -.
DR   eggNOG; KOG1616; Eukaryota.
DR   HOGENOM; CLU_445500_0_0_1; -.
DR   OrthoDB; 120305at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 6.20.250.60; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR006828; ASC_dom.
DR   InterPro; IPR037256; ASC_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR   PANTHER; PTHR10343:SF84; ALICORN, ISOFORM A; 1.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF04739; AMPKBI; 1.
DR   SMART; SM01010; AMPKBI; 1.
DR   SUPFAM; SSF160219; AMPKBI-like; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT   DOMAIN          538..686
FT                   /note="Association with the SNF1 complex (ASC)"
FT                   /evidence="ECO:0000259|SMART:SM01010"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..297
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  77405 MW;  B9163785FFE0DE61 CRC64;
     MGNNTSTTGS TGSGIIRRGS ESTRKSTASA NYNNLNGKDH FNDNRVRKSS AGKNTNSLDE
     EFSDLILHQV VTKPSNSNLV PQQSQSQSQS SQQPPPRQQQ QKKQLPHNQF SNDLIEDEFN
     ELNEVLVETD STALQRNILP DDGFENENSS SSDTTPTTND STTVTDDMDI DEPFPQDYDA
     GSDVEDEDEI MNNAPDRSTT PTPDLTKVDF TKITSQKPPS LSNENVSVPP PAQMLSAASV
     ARSVHSPSPN LENQKYLQQR PSKSMKTDQS TTPQNHNYHH HHHHNQHNHH YHNHNNHNRQ
     KQQILIPIEI KWVNVTKEQI NKIAIIGSFS NWRDVIKMYP STSHPNEFVT TINLPLGVHK
     LLYIINNEYR VSDQLPTATD QEGIFFNWFE VIDDTHLFNH SMNQPNHIGA STDYDANIIK
     FEEPAMAQSP QYQQQQQQQH VYGASGSPMN NITPRPAGKY DVDRIHQKSA ELMHKISKES
     TSEFEHVEFI EDTQSDQLLP PQVTQPNDIY GTSYENTQYQ PFDLSSNNSN SFLAANAVNE
     PTYEYSSEIP EMFINYDYFK LKPSNYELPE PPQLPPHLNN VLLNKISSSG SSSSSGSVHT
     HIPTNISSNS GGLSSTSTIN SIKRPPLRRA DSSYYASSKE SYHLQIPNHV ILNHLMTTSI
     KNDVLTVACI TRYSGKFVTQ IMHSPADK
//
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