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Database: UniProt
Entry: A0A168MZ21_ABSGL
LinkDB: A0A168MZ21_ABSGL
Original site: A0A168MZ21_ABSGL 
ID   A0A168MZ21_ABSGL        Unreviewed;       592 AA.
AC   A0A168MZ21;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=RGS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=ABSGL_05100.1 scaffold 6272 {ECO:0000313|EMBL:SAL99486.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL99486.1};
RN   [1] {ECO:0000313|EMBL:SAL99486.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL99486.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT552697; SAL99486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168MZ21; -.
DR   STRING; 4829.A0A168MZ21; -.
DR   InParanoid; A0A168MZ21; -.
DR   OMA; ADVNIDH; -.
DR   OrthoDB; 1364107at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd04371; DEP; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF192; REGULATOR OF G-PROTEIN SIGNALING 20; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00049; DEP; 2.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700}.
FT   DOMAIN          218..288
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          369..540
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   REGION          305..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  66969 MW;  9567FA9CFC182054 CRC64;
     MPFSNLELSS TYTTTMKLTG DGSRPFAKDV FDLFSAMILQ LTLGDHRSFF RTYPSTFTTD
     EAAACLKALK FSHVVKTPEP NNNGYRLTRT TTTFYMERVI AKALLQQFLN TRLIMIATDT
     TARTVKDKGI WALTSKGKRM IIDFGERAFV PVDHMAPHLA TINTISVFAL DRIKETDQLA
     FERDNITLCF KIMMTKIPLE NILADDVGGL QHHYLEEYTH TFFGYQCFEW LMQYTTVVNR
     GEADMVAGEL VLYGWIAHIL DKSDLGNNTF DDSVLFRTSR NALYHITERG RLVLGWADSR
     SSAKSVSSTS SQKESNGKTK KQQKQQLQQL QHQSLTSIYA SGEHPRPASI SNSETDVLTS
     NDDAAQFVRL RQILEDPLLR MYFRIYLKDN FCDENINFWV DYFAMRKKKK AQHTKNGLKD
     MISDSYAIYD TYLKSKAVHE VNIDHTLRKN IDALVKSTFS IVYEPKKHSN SPSSSAPPFA
     SPAVTPHSAT TTAISVNAPL AQCLHDLMKL YDQVNDHLCK MMAQDSVPRF LRTSKYQKLL
     NAHLPPLPPP KPTPEQSQQQ ASSSTTNQDP NIQLASVTQL TDGIKTLACK ED
//
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