ID A0A0Q4V3L5_9MICO Unreviewed; 765 AA.
AC A0A0Q4V3L5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cyclase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF23_10755 {ECO:0000313|EMBL:KQO62280.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO62280.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO62280.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62280.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO62280.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62280.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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:KQO62280.1}.
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DR EMBL; LMMJ01000009; KQO62280.1; -; Genomic_DNA.
DR RefSeq; WP_055953863.1; NZ_LMMJ01000009.1.
DR AlphaFoldDB; A0A0Q4V3L5; -.
DR STRING; 1736311.ASF23_10755; -.
DR OrthoDB; 9806704at2; -.
DR Proteomes; UP000050821; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR PANTHER; PTHR45655:SF13; SOLUBLE GUANYLATE CYCLASE GCY-35-RELATED; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050821};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 499..551
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 591..718
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 82672 MW; 64AE75AC77B7AF52 CRC64;
MTVPPQQPQH QPASGPAPAP GGDDLRTAVG QTDPIPPTSG SDGQQSGPRV IEDAPRRTGR
WRAFRTTGVL DIQSKLLIML LAVSILAALV VGAVGYVNGR NSLQDAAFQQ VTSLRESRAR
EIERTFSDIS GAIVLDSRNQ SAIGATKAFT SGFAALQDEN PTAAEQRSVA NYYSDQFVPQ
LDKATASTAD PKQFTPTSNA QTYLQSKYTA PFDDYDKSLA TDDAGDGSAW SAAHAEYQDY
FREQVDQLGY EDVLLLNTTG DVVYSAYSGP DLGTNVETGP YRDSNLASGY QKALQLTSTD
AYAATDFEAY TPSLGAPTAW VFSPVGDNGQ IIGVLAVQVP TETINAVMTG NQGWKSDGLG
NTGESYLVGR DRTMRSTSRQ LVEHPKQYQQ DVISAGEAPA DAREQVRDKS SILRQSVTTT
PVTRALQGKT GTVITSDYRG RETLSAYAPV EVDGLHWVIV AQVDTSEAFQ PVDTFTRTLG
LSLVGIIVLV CLLALLLAQV FVRPIRRLQT AVNRVSAGDI GVEVAAKPGD EIGDLGLAFN
DMSRSLKIKQ DLLDDQRRQN DQLLLTMMPV EVAKRYKQGD ENIAEEHQDV AVIFADIIGI
DDFSKGFGAS DGLQLVNGIW RSFDEAAARI GIERVRSTRS GYLASCGLTV PRVDYARRMV
EFTNELQTIL ERFNAQHGSS VGLRAGLDTG RVTSGLVGPS RAVYDMWGDA VNLAYRVQGI
APTPGVFATQ RVVDQLGDTV PMHEEGTVET QGGPQRVWKL DRRAS
//
