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Database: UniProt
Entry: A0A367KSG8_RHIST
LinkDB: A0A367KSG8_RHIST
Original site: A0A367KSG8_RHIST 
ID   A0A367KSG8_RHIST        Unreviewed;       674 AA.
AC   A0A367KSG8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=CU098_012956 {ECO:0000313|EMBL:RCI05080.1};
OS   Rhizopus stolonifer (Rhizopus nigricans).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI05080.1, ECO:0000313|Proteomes:UP000253551};
RN   [1] {ECO:0000313|EMBL:RCI05080.1, ECO:0000313|Proteomes:UP000253551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI05080.1,
RC   ECO:0000313|Proteomes:UP000253551};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCI05080.1}.
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DR   EMBL; PJQM01000488; RCI05080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367KSG8; -.
DR   STRING; 4846.A0A367KSG8; -.
DR   EnsemblFungi; RCI05080; RCI05080; CU098_012956.
DR   Proteomes; UP000253551; 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:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0000165; P:MAPK cascade; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06627; STKc_Cdc7_like; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR003096; SM22_calponin.
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; PF00307; CH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000253551};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          14..120
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          357..608
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          166..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         674
FT                   /evidence="ECO:0000313|EMBL:RCI05080.1"
SQ   SEQUENCE   674 AA;  75340 MW;  D78B6EDD57C0D8D6 CRC64;
     MTTTTITTLP VFQQEPEEIV KQFLIETLDI KELPKGSLQE ILKDGILLCE FIKRFSPNEC
     IVKNEGHTKF AYQDNIGQFL RVAESLHIPQ SDLFQTVDLL EGKRMQSVIS CLLAIKRIMS
     ERKVIPTKQT TKFPTTGRKK SSKNLLLLAS AYPTLTHATT CNLLQRSGRT SPSSIKQTSE
     KKSPVHQYMS SATKNQANRT SVFDWPKKPI DARSEQKKQQ TNGGYVKLQV QMITTNNLTM
     ASEPKAKARR SSSSENSLKS EERLCVEKPV PLKAESARET RKSLAPPIPK PSKSTPLVAA
     TNVTVTTTKG CCDQKAAAEN NLQYYNNIES ANRKTSLKKM GSCAITVESD DGATAVYALG
     RSIGKGQFGE VFGGLNMDTG EYVAIKRIKR NQMDCDDMNE VGVLQHLNNE HIVRYKGFAK
     DKEFLNIILE YVEMGSLHNN IKAFGKFPEK LAASYTYKIL SGLHYLHSKD VIHCDLKAAN
     ILTTKTGGLK LTDFGVSLSL KMKDDETTGE PAGTPNWMAP EVIKFAGASA KSDIWSLGCT
     IVEMLTGKPP YANMPSFAAL YRIVEDDEPP IPKNLKLSEE AMDFLKSCFK KNPEDRPSAL
     ELMKSKWMES YFRQDKTLLL SPPSSPDYTT KRSKSEEADI DRKHQFIDYQ THKTGEECSG
     CFSLMKSVWA KYCQ
//
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