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Database: UniProt
Entry: A0A0T2L128_9MICO
LinkDB: A0A0T2L128_9MICO
Original site: A0A0T2L128_9MICO 
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}.
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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
//
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