ID   A0A2G4T9S5_RHIZD        Unreviewed;       777 AA.
AC   A0A2G4T9S5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=RNI-like protein {ECO:0000313|EMBL:PHZ17745.1};
GN   ORFNames=RHIMIDRAFT_233167 {ECO:0000313|EMBL:PHZ17745.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ17745.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ17745.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ17745.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; KZ303842; PHZ17745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4T9S5; -.
DR   STRING; 1340429.A0A2G4T9S5; -.
DR   OrthoDB; 1330350at2759; -.
DR   Proteomes; UP000242254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   PANTHER; PTHR45638:SF11; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 10.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   4: Predicted;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          33..150
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          191..294
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          363..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  86934 MW;  ED0D26FD714BC98E CRC64;
     MLDIQKTDTA WHTASHNTVP PELLRSLRHH SLFQRANNEN FLEKIACRMH LRTYGPRDVI
     VVEGEPAKAM FFLLRGSVDV CSADFERIYA NLSQGSCFGE IGILYSMPRT ATVIARTKCI
     VASLTAEEVN NLLPQYPEVE KMLRFEAEER LAVLSKSKNL GVKEKVSLKP MTERNIEDFT
     GIRQLLQKIP FFQGCPEEFL HLISLKVEPR HYAPNAVIIS KGEYGNELIF IISGTVELTK
     TDDSGILVPI TRLSQGDYFG DISVLLNTPR ATDARAVTAL ELYILKKSDF MDVVHHFPDL
     LGRFKAMAEI SLSHLQSMTG AYQMRGVEEA IDTPISPRTN HEQLSPEGLS SLTIPTNSVC
     STTADQDPTL LPPTPTSNLK KTETRRRRAS VAVWSDPNLV ALANRHIKPD KHETQQTKMM
     IESTQPQPKI SQPVIKGQLS LFTEDILSRI VNCLDFTSIL QLSIVSKQCR EFIQQNSNVL
     KSLDWSSMHK KITDSNVDHL VQFTGSRVRY LNLSQCFYLT DDGFKVLVEN LPNVEVMDLS
     SCWLLTDKSL ALLGTTCPQL TRLNLSNCRK ISDIGVFRLL DAKASNSYPM LEELSVSYCK
     KLSDTTMRHL ASYCSNTLQL LNIQRCTRIT DLGFLAWTST CFPQLQELNL NDCSFLTDQA
     IAYLISATPN LKRLSLSFCC ALSDSAIERL ATLKQLEYLD VSFCGAAVSD VSVRTLLASQ
     SMNSLNIRGC VRVTDTTVYS ILELGQLRML NISQCPGISS NAKEAIKAHA KLQELIV
//