ID A0A1E7JQ88_9ACTN Unreviewed; 1343 AA.
AC A0A1E7JQ88;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=PAS domain S-box protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AN215_13105 {ECO:0000313|EMBL:OEU90405.1};
OS Streptomyces abyssalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU90405.1, ECO:0000313|Proteomes:UP000176087};
RN [1] {ECO:0000313|EMBL:OEU90405.1, ECO:0000313|Proteomes:UP000176087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU90405.1,
RC ECO:0000313|Proteomes:UP000176087};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEU90405.1}.
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DR EMBL; LJGT01000038; OEU90405.1; -; Genomic_DNA.
DR RefSeq; WP_070031158.1; NZ_LJGT01000038.1.
DR STRING; 933944.AN215_13105; -.
DR PATRIC; fig|933944.6.peg.5184; -.
DR OrthoDB; 7053013at2; -.
DR Proteomes; UP000176087; Unassembled WGS sequence.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000176087}.
FT DOMAIN 161..236
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1220..1337
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 67..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1269
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1343 AA; 138176 MW; DF50FE93B8167D34 CRC64;
MSSRPSRGAA RLAAILDALP DALLLVNCNG TVVNANTIAL EAFEAPGTAL VGRGLLDLLP
EFDSKRIPGS MRRPDEAAAE LEERQRPTRM VARRTDGSEF YVEVTSANLE DGRTPYASAF
EAAFADHGPG SGNSYTGDEL LMLVVRDLTG TLDTEAELAR QQRQTEMILR AASEGVIGVD
TEGLIVLVNP AAAQILGYRA GDLGGQEMHS LLLHSRPDGN PLPYEETTLS DTLKSGRKHR
VRAGHVLWAK DGQAVPVDIT TAPVRDGEQL VGAVVTFSDR RAQEALAGRH DQLLAVLQDS
LRGPLDQLRD ELSGLAADPA GQLWPEANQI LHHLAAGYAR MTTLVDNVLG YQRLDAGREK
LRREMTSLDS VVANGVEGAV ELIGPGRAQF AVHAPPIEAE VDGERLTTAL AHLIADVAGV
DATGNAPAVT PGLDTTIVVA AAQRGEVVRI EVRGPYAGGN PVHLPIVRGT VERHGGVLQT
HEVPGAGGSA YVLEVPLKAD SAGSGVDAGA SGASGDDRTS GQVQGQDQGQ GAADGTGAGT
GHAQRGREGR ENETTVMPVP AQPVRGTEAP AGAQASAAGA WTGTGDVSGA APAAGIPDQF
QARHTQGQPA GGHEGQAVPT GRRRGRPSPA EAHQQDQQQA QQSQQVAAAQ GGAVTELPPS
GPAGPDAGEA AGATVPQQAG AGRRSRRALA SPAQAGADGT AGQGPGQGQG PEQGQVEGHG
QGAEAEEAAA AQQLPAQQQA QPGTGRRGRR PVQGQGQGQP VQAQPVQAQP VQGDEGADAA
QPGGRRARRL AQAQTEGDAN PQGAQGAQGV QFAAPPGQPQ PGNAPQSGNA PQSGQNGASS
ANAAARAELP GGQQNGMPQQ LPPEQAPAQQ SQAPAQAQGQ AQGQGAGPQP ASAQEAEAEQ
EAEPQPVEHS VVAASPILGG GPLPQNVSQP RGLPMPGAPS AEEQASYETG QHRVQTLGQG
VPVTPGMTEQ RAGGPQSYGH QVAHAPTPSP RQAHAPAPAT AIPSTPSTPP GSGRRRKLAA
PAQPGGGQPH GKQAAGQPAQ GRTAHAPGQA GPANPPPARE FTIGAPAAGT AEGPEPLDGP
NSPVEMSDGR GVPVPPQAVD DELPPEPLDN PRRLLVWPEP DAATQRALSE QGYRPVIVHS
REEVDAQIAA YPAALFVDPL TGPITRTALQ SLRTAAVAAE VPVMVTSGLG QATREAAYGA
DPAVLLKALA PRDSEQHPPR VLLVEERPPI AVALAASLER RGIQVAHAQT DEAAVNVAAQ
MRPNLVVMDV MQVRTRRTGI IDWLRVNGLL TRTPFVIYTS ADMNPADLPR LATGETVLFL
AERSTADEVQ RRIVDLLTKI GTN
//
