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Database: UniProt
Entry: A0A1C4QN19_9ACTN
LinkDB: A0A1C4QN19_9ACTN
Original site: A0A1C4QN19_9ACTN 
ID   A0A1C4QN19_9ACTN        Unreviewed;       917 AA.
AC   A0A1C4QN19;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=PAS domain S-box-containing protein {ECO:0000313|EMBL:SCE24094.1};
GN   ORFNames=GA0115242_1268140 {ECO:0000313|EMBL:SCE24094.1};
OS   Streptomyces sp. SolWspMP-5a-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCE24094.1, ECO:0000313|Proteomes:UP000199131};
RN   [1] {ECO:0000313|EMBL:SCE24094.1, ECO:0000313|Proteomes:UP000199131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCE24094.1,
RC   ECO:0000313|Proteomes:UP000199131};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMCI01000250; SCE24094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4QN19; -.
DR   OrthoDB; 9807247at2; -.
DR   Proteomes; UP000199131; Unassembled WGS sequence.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR   PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
FT   DOMAIN          202..232
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  97157 MW;  38EE4FF2AF848D6D CRC64;
     MTTGLIPGAN PPDHGPTGGL PQQRRENAGP AALHVDNRPR SSVITARAAA SFEPVGRSVA
     TARSFVRDTL QGWGFSDIVD DAVVLTSELV TNAVVHAGTA ADVLCLRSDD GVRIEVADHY
     PEREIPLQGS PATMGSPDRE GGRGLQLCAA LAGRWGVDYT PTHKQVWFQL HLPERAVGTR
     AAGPSLPADL LPLADGRVRV AVVQIDRTGA ISAWNEDAEE LFGYPAEQVV GKPLTDLAAW
     PHTPGTSTGI VEALQLSRWE GSYGIRGADG RVTPVYASHL RVRDTGGEPS TVCLLVRDHE
     RAVLQTPTRM ASSDGSGGSE SQSADPFEVF IGSPAPDDLD GLLQRTVERA RDMLDGDSAF
     LLLATDDETE LEVRASTGLP SARQRFARVP VEAGPGRYGS ARMPAVHDDL TAVPGAVPLL
     SGTGMRSVVT VPLKVEGRLT GSLGVAAEGP GRYSNEEALR LQFAADRIAL AVESARLGEL
     ERLRRGSLSF LVEASDLLAG TLDRDQTLAL MAQMTVPTLA TWCAVYTIAD QASEPYLSYV
     LHEDEELIDG IKSLLSKIAP PDPVPTPGAR VWPAPGEVAH QAALRSSMRS LGLSGGPTHQ
     VASSIGPTLA TASAVGGETV VLPLVARNRV IGMLTLGKPT DEHFRQEILE LAEDLSRRAA
     LALDNARLYS ERTAISQSLQ RSLLPPELPV IDGVEVEVIY RAAGEGNEVG GDFYDLFPIS
     DGAYGFAIGD VCGTGPNAAA VTGLARHALR LLAREGLSGP AVLERLNSAI LDEGARSRFL
     TLLYGELRPQ EDGSAELKVV CAGHPLPLRL RQDGTVEPAA EPQPLLGVME DLELYEQRVT
     LDPGDVLLCV TDGVTERREG TRMLGDDGLT DVLTTCTGLT AGAVAARVMR AVERFASDAP
     SDDMAILAMR VPGLQKD
//
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