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Database: UniProt
Entry: G7E1U1_MIXOS
LinkDB: G7E1U1_MIXOS
Original site: G7E1U1_MIXOS 
ID   G7E1U1_MIXOS            Unreviewed;      1616 AA.
AC   G7E1U1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
GN   Name=Mo03471 {ECO:0000313|EMBL:GAA96801.1};
GN   ORFNames=E5Q_03471 {ECO:0000313|EMBL:GAA96801.1};
OS   Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC   Mixiales; Mixiaceae; Mixia.
OX   NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA96801.1, ECO:0000313|Proteomes:UP000009131};
RN   [1] {ECO:0000313|Proteomes:UP000009131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC   {ECO:0000313|Proteomes:UP000009131};
RX   PubMed=21478649; DOI=10.2323/jgam.57.63;
RA   Nishida H., Nagatsuka Y., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL   J. Gen. Appl. Microbiol. 57:63-67(2011).
CC   -!- SIMILARITY: Belongs to the Rho GDI family.
CC       {ECO:0000256|ARBA:ARBA00009758}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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:GAA96801.1}.
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DR   EMBL; BABT02000106; GAA96801.1; -; Genomic_DNA.
DR   STRING; 764103.G7E1U1; -.
DR   eggNOG; KOG0220; Eukaryota.
DR   eggNOG; KOG1113; Eukaryota.
DR   eggNOG; KOG3205; Eukaryota.
DR   HOGENOM; CLU_242929_0_0_1; -.
DR   InParanoid; G7E1U1; -.
DR   Proteomes; UP000009131; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12098; DD_R_ScPKA-like; 1.
DR   Gene3D; 1.10.1420.10; -; 2.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.70.50.30; Coagulation Factor XIII, subunit A, domain 1; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000406; Rho_GDI.
DR   InterPro; IPR024792; RhoGDI_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR   PANTHER; PTHR11361:SF21; MUTS PROTEIN HOMOLOG 4; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF02115; Rho_GDI; 1.
DR   Pfam; PF02197; RIIa; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP {ECO:0000256|ARBA:ARBA00023149};
KW   cAMP-binding {ECO:0000256|ARBA:ARBA00022566};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1123..1263
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1266..1386
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1091
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1616 AA;  176767 MW;  6469C7A5864ADDFB CRC64;
     MSVRPPSTRP PTAALSIRRP TTAASTRETT NGGDADWVVA VFEAKGSHRQ VAVAAIDVER
     SLCFLSQVCD TQTYVKTLHI IQQRYPATLV LPSQVTTTML TVDSPSASSV GPSPVLSSLT
     ILSRLIKNNF EMTPLHGLAK KHWAIDQGIE LIDKLALDEP AKMTLLATVT ENTLALAAFA
     GLIRHLEGHH RILYANNSLK IVFTALEGTM VLGTDTLRDL ELLQNTMDGS SKKTLFDLLN
     SCMTPMGTRL LRNNITSPSA DRFTLNKRLD AVQELVINRD TLETCRQALH KLAKTDYDKV
     IGKISTNKPR DFRGQGDPAR EAEKKISTVL QLRTLLESLP SIALSIDASS SDLLKDLASG
     LRGQADVILD SLRDTINEDV VTSFQEGKGQ LALRNVRVYA IRSERKLLLD VARVTYKENM
     QDLLDMANEM SAIAGTTVNL VPVSSGFAFS CSKDGLPGGV LPKGCTEGKA KSGKRIQFAS
     ADLKKRNARL QQSLEEVFLL SDEAIDELIE GIKQHLAFLF QCVEAISTLD VIASLAYVAT
     IEGWTRPEFE NAMAIKAGRH PLVERYQMRD RNDFIPNDTY ISNNRSFQLI TGINAAGKTV
     FTKQVALLVI MAQLGSFVPA DLASFGIHDA LLTRLNNDDD LGKSLSTFAV EMRSASMITL
     ALDAFRAPLV VIDELGRGTD PVAGFGLCHA IAEEIIKKRA FCLFVTHFRE LTLSLFGYSN
     VAQFHLEAKA RRSSSAFSFE YRHHVQQGSN AETHYGSLSD SLPVCSPDAE VKTGLEAAKL
     VDLPSSMLDF AHQVSDKLAH LERKSRIDAQ STRDEVRRKE MLRIVDQLEE LALARELSDV
     EIGDRMRVLQ ADLVEGLVRS SFAGRGQIKA DVKLENRPAC AGRWSTFVAV MTSTYSSILN
     DLNRDVARNQ PADIWQFCAN WFNARLEEQR AATRPVERSV TPADQSRPIS PPANVIPAMR
     SSPTKREVIR KKSNPSMLGA AYSFGGLGSG IAPADPAPSP FSETPPALKH QTADSFGHDH
     PVVSGNGRAN SGLRNEMPSA WQRSGRPRAP MTSAPSDDEG DSGGDDGPSS PGPPPNYNIG
     RRTSVSAESL DPDAAQTALP KTVIPKTASQ RQRIEHSIEH NLLFRNLDED QYNDVLNAMK
     EVRVPTGSEV IVQGAVGDYF YVVEEGVFEV WVRPSSAGTY GPDGQRASGP NYGKDSDAKH
     VATIESGGSF GELALMYNAP RSATVVAVSA TSTLWALDRV TFRSILMEHT SRKRRMYETF
     LSEVPILVSL ESHERAKIAD ALEARIYEEG EAIVKEGEVG KNFYIIESGS CEVTKRRPTG
     EERVVILRKG DYFGELALLN SAPRAATVRA IGDRVRVATL GSRAFHRLLG PCVEILQRRA
     GSYNSAPAAE PRRGLPGNTR SIQPDTAGPR SRGLGMVTAE QHWNRHHARP QVTMTDVDDA
     DLVSESQYKA PAAPKDLEKL EFRDDSLKKQ EEALGVGANA TGKARVTVLA LVLTSDSRPE
     PIVLDLTKPL PEAPLVIKEG ATYTAELRFQ VEDALVSGLR YLQVVKRAGI KVDRIEAMIG
     SFAPSAQVLS KKFESEEAPS GMIVRTGTYN VRSRCTDDDG TICADFAWSF KIGKDW
//
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