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Database: UniProt
Entry: A0A0J6YK82_COCIT
LinkDB: A0A0J6YK82_COCIT
Original site: A0A0J6YK82_COCIT 
ID   A0A0J6YK82_COCIT        Unreviewed;      1430 AA.
AC   A0A0J6YK82;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0000259|Pfam:PF16561};
GN   ORFNames=CIRG_08722 {ECO:0000313|EMBL:KMP09041.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP09041.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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DR   EMBL; DS028098; KMP09041.1; -; Genomic_DNA.
DR   STRING; 404692.A0A0J6YK82; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1405..1422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..103
FT                   /note="AMP-activated protein kinase glycogen-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16561"
FT   REGION          83..1395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..696
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..995
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1028..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1072
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1119..1142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1222..1238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1332..1347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1430 AA;  150738 MW;  A4E1B9C4CD60A049 CRC64;
     MTEDSKQSVR IAVRRPTSTP SIFLVASFTD PAWDPVELEA KPVTSADATS EAYEFSKSFE
     LAPGKYQYKF RAGSGDAWFC DTDVPTEVDN DGNMNNVLPV ETASDSKKDD PQAGQSKSDN
     TTENAETVVA SDETTEKAAA DKESNGVNGI VAEKADPEPK EASIPAEEAP EKAEKESTGG
     EDVAEQPTTV SEAIAKGTPS DLKPADDSQP KADIKDEDVS VNGGPVEKKL EVQEAETESP
     QPEKKEPEVS PDSSADPISS ATEAESPEQA EPEPSEPKAE EPKAPVEPEI QPTSEVEKQA
     EATEPKDESP AVLNPEAPQQ LTETAKDLES RPQTPASMSS STRSLNPAAP AFVPGKFTPV
     SVPNPVETDD AAPKDDKESQ PPAPEEPKVA EKVPEASTAG DEVDKDKEEV VASSKPEEDV
     AQTTTTTAEE PKETPAAEQP AMDAVKEVEK PAEPAAPEQT EEPAEEAPKV EKAPEVETAA
     AAVSTDPIPE ATAEAVTEDK EEEKNVSTTE APSEPLAENV TASATETVEE SAQKDDEVVP
     SSKTEIEEKE VQQQEKPVDE VPVAEDSPAE PEPVKASTEP ADEKAAPTEP PAAKNAADGE
     ILAEKDDAPV KEPTSGDEEP CDEQIASTAG TTPIEAEPAS EPVKEDEKRD DEARLPAEPA
     PEEKAAVADA KDSPAEATDG VAQEKQAEEP EPQASKTDAD DVIQTEAAEA EPQPEEQNAD
     AKQDQETATS GVESAEPATA SEAAVDEDTV ATKKLKEAEV ADTVAAVEPV VEKEDTVAPS
     PAPAQEPAET PNEQVEAQED VVEDEPARDA AAEKAVEQVP QKSMDPVETL DVKEVTPVEP
     SDKAPVPDTP AVVDEQPEVT APADAEKEAT EVQQEPASKP DNEPEPQPEA PTSTEALEPS
     ADPEPKAETP EVLEAEINAP EEPVVQDDVK EPEVPVTAEP VPAAKEESKP ADEPEPSTDA
     TASEKIEAEP AVDLKAEETP ADTQPEEKVD PTPVKDQSEE TPVTVVDEPT TGGEEAGASA
     APIADEPAEA EKPADLEKAE EPVEVSNDVT PTPETKAISE TPDDDESKPK ESPVQPAPEP
     ESTPAPPVVE DKAEPQEESN AADVNVAVSA SDEPAEKSVG VPVQKDEPEP LPKHEEEAKD
     EPYTPPAGPV ASEEPQVEPV TAETLPKDSD VTEDAPKANG VNPVVAVEEV AESTPESLPL
     AADTSHVTVE DAPKDETHVQ DKSLPQAPSQ TTETAIPEES PAQPLESTPV AKSEPPVVEP
     VVQQKVIDDN VATMPANEET KKDVPSQREE QPENPAKSAE VIPPQAAVKP AEPAPADAGS
     AKEPVSQQAP IADARSEPSS MSDANAKSAT PIVDAIKAAT AAEPASKDDA SKPVAKDADE
     PQRPPTANQS VTSLTTHKRE SFFRALWRAV FLNFFGGLFG AFRRRERPPQ
//
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