ID A0A0T2L128_9MICO Unreviewed; 713 AA.
AC A0A0T2L128;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cyclase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASD65_15520 {ECO:0000313|EMBL:KRA25671.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA25671.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA25671.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA25671.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA25671.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA25671.1,
RC ECO:0000313|Proteomes:UP000051216};
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 -!- 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:KRA25671.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMGU01000001; KRA25671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T2L128; -.
DR STRING; 1736570.ASD65_15520; -.
DR Proteomes; UP000051216; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..495
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 535..662
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 713 AA; 77346 MW; 5AEC7E46F86484B5 CRC64;
MWVGRPRARR RAGLSIYSIL LIMLLSVSVL SSIVVGIIGY ANGTQALRTI AYEKLVEIRE
NRAREVTELF TTIENAVRLG AMNETSTQAA RAFADGFAQL DQQPLDKDQS AQLRDYYDGT
FAAQLSDATG TVVDGATFTP KDAAERYLQY HYVIPYASWE EAILSEDAGD GSAWSAAHAK
YHPYFRAMTE LQGFEDVLMI DASGNVVYTA YKGVDLGTNL LDGPYRLSNL ADAYRESMSR
NIVGDVVLAD FAPYSPSLGN PAGWAVTPIA ADGEVIGALA IELPIDRINE VMTVGRAWEQ
NGLGQTGETY LVGRDQLMRS VSRALIESPD TYVKDAVGAG LSPAAAALGL RNGDTLMQQD
VTSVAVTRAL AGESGTMLDT DYLGRESLTA YAPLAVDSLP WIIIAQETST EALVPVDDFT
RNLILSTAGM IIFVCLLSLV LAQVFVRPLR RLKSAAQRIA AGEEGVQVDA GSSDELADVA
TAFNDMSRSL QVKSGLIEEH EKANERLILS FMPEGMASRY KHGDDAITQD NDDVTVIFAD
IVGFEALAMS LSSEEAVTRL NDLIRTFDEA AEKYGVERVR TTRQSYLASC GLGTPRVDNA
RRAVEFAMEL STILERYSAQ QGVELGLRAG LDSGKVTSGL IGRARVVYDM WGDAVNLAFR
VQGDSDEPGI YVTQRVADRI PDTIPIRPAG EVETQSGTQR VWRIETAVTV VEG
//