ID A0A176VH12_MARPO Unreviewed; 1648 AA.
AC A0A176VH12;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=AXG93_3756s1170 {ECO:0000313|EMBL:OAE19611.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19611.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19611.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE19611.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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:OAE19611.1}.
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DR EMBL; LVLJ01003810; OAE19611.1; -; Genomic_DNA.
DR OrthoDB; 297509at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
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; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR PANTHER; PTHR43336:SF3; GUANYLATE CYCLASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43336; OXYGEN SENSOR HISTIDINE KINASE RESPONSE REGULATOR DEVS/DOSS; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU363067};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR623088-3,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1025..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1267..1289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..512
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 91..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ SEQUENCE 1648 AA; 182900 MW; B1D56C34C7EA54EE CRC64;
MLSSGSDASD GHTAAVGWAR LAVMRGTESF MRRGFGPSAD FESEKEAFGR AFSFMSGYSD
IKWPLYPTVH QQCTTLRTDA FMHACFEGGK PELKDDKGKD QEENDEAKNK RPRDLRIPLL
NLERAREYVP PASPTEKTAS DSEMLIISEL PNIGQPDFSF SPVLEREMVE KIFRELGLFD
NFPLDVKKVR AFTNAMVMRY QPNPYHNFRH ACDVLHAVYL ILTLVDGRKK LSHLEVFALA
LAALCHDVDH PGLTNAFLVA TYDPLALRYN DRAVLESHHA ATCFITMRGN DSLNLLAGLS
EEEQRHMRKL MIVLILATDM GEHARILREV GERVQDLRPF EQSPFYTPPG CLSPILRDAE
SSSSGNTTAG AKSSDAPPSP KRLPDKVYKN PLSPSPPIQS TSDVMLLIQL IIKCADISNV
VKPFFLSKRW AALLLLEWFR QGEIEKQLGL PISKFMDRED PSTLMAMTCG CIDYIAKPMY
EVMTKLLPRM HENVLVNLNL NRQMWSTFST NGRRASETAQ QILGPFAPPP IPKGEAVQEG
YQQDHSKLEG KLVATFSGQY VSSDVPSRKL ESSPSAKSLG SVSEDSEETV ENVEDSPILS
VTDRSSEFSR LGSEAGSSVK TSPQFLSRAG TEAPSSPQSP LQASQEQRGS PSPGVQYRLS
PRGPGSPSVP VTQISGNPES PGYRETYGPG GSQPAAMEVP FVQKSPHEPV AVDVDVATSQ
QSADVIAPLS KPQALQVKQP VVPTVSRGVH FDDSELTASE RSELSSSIQS GSSPDLALRV
SFVAINPDSD SVKVLIEQSD PLSTATIEQR DPDSPRMTGL EPFLEEVAAS SSESKAEPET
EDEYNQRYEA PLSLLFGAPT REELMLPAKI GKDKNASLVS ALLPGANNLV NDRKQNAWEQ
MAFRSPSEQA ASRGSILTTV PSFANSDGDL EKSSSLRKGP PPGFWEALRT HPRVNRLNRA
LESKTWNALL IVATLVALFA DDVVKGFLPK HADVYESHIL TACLSLFLAE SALLCIFRDR
YFFSFFFWLD MLGSVSLVPL VIGITAQNLV IARTGRAAKT VTRFSKTLQA SHIQQQIVHH
IPVLRVFKFF GFKRDSTLES PDYEEEEKFL SKPSQLWSRL AELTSQKLIL GVLIIMILTP
YFNNSEKDLA PLVSLDPLDD YLIGSPNFNL TVERVINMTK RHGYNLLYLG VKASCRSIKE
GGYSYCLGID VAGVEKYQQI LPNVDEEPDG RQAAQEEFRP TELISVTSDS SRAQAYYSIK
KKSRFKYGMN IAMTVLILLL LAAWCFFLSR DSNRLLIQPI ERMVQFVKEL AEDPVSFAGK
TVVKPTGDSS KIMETFYVEA ALVKIASLTK VALGDAGMDI LSVNLKGSEF NHATECLQED
VMMFVNRIAD VVHNKVVLHS GFPNKNIGDA FLIVWKKTVS DNTNKSRATS FADRALRAFL
DIIQSIETSQ SLAEFAKHPA IQKRMPGKLQ TFVFKRFSCV SLDYVGPPME GIWVVRAIGS
AHKVDPSYLS PHVNMASRLE AATKQYGVML LISETVIAHL TKSTLRDSCR KLDRVTVKGS
QDPMVLYTFD IPLFQQDLRG NPQEYRDIFE EAVDSYIDGD WDIALERLQE CQTLWPTDKP
ATVLLTFMAS HNNIAPENWA GFRELTEK
//
