ID K1XBR3_MARBU Unreviewed; 929 AA.
AC K1XBR3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000313|EMBL:EKD18143.1};
GN ORFNames=MBM_03915 {ECO:0000313|EMBL:EKD18143.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD18143.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD18143.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18143.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH921434; EKD18143.1; -; Genomic_DNA.
DR RefSeq; XP_007291804.1; XM_007291742.1.
DR AlphaFoldDB; K1XBR3; -.
DR STRING; 1072389.K1XBR3; -.
DR GeneID; 18759850; -.
DR KEGG; mbe:MBM_03915; -.
DR eggNOG; KOG0498; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_006113_0_0_1; -.
DR InParanoid; K1XBR3; -.
DR OMA; RMKSVWD; -.
DR OrthoDB; 1330350at2759; -.
DR Proteomes; UP000006753; 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 CDD; cd09917; F-box_SF; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
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; PF16643; cNMPbd_u2; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00367; LRR_CC; 8.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50181; FBOX; 1.
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:UP000006753};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 65..182
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 273..400
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 543..598
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 397..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 102893 MW; 5E6A59719A769F6E CRC64;
MRRNRGGPSS SFRTNGAPIP DSLSLIRSFN IETNPTRPIR PSPLTASTIP DMPLDIVDRI
RSFPLFLSAP DSFLAAIGKH LRPQVHSPHD IILTEGDEAK AMYWLVRGAV AVTSRDGEAT
YAELRPGSFF GEIGILMDVP RTATILARTK CLLVVLKKED LRQELPKFPE MEKAIMDEAQ
ERLTILNKKR KESGKGPKLI STVLPSRGGK LLAREPAPGE VSTGDVGVIE KGAVINTKKR
KSPSPQGIED PAAGSALGSG FINVRKTLKD LPLFSTLPTE ILHFLGLSTQ PKTYPPFTDI
ILQGSPGNEI YFIVRGEAEV IHETTNGQTQ PPRGSYIRPR LKQGQYFGEV ASLALAPRRT
ATVRSITTVE CLMISGEVLE ELWRRCSPDI RRQVEQTAKT RIGKSEDQDV HMVDIDDPST
NSLENHERPI TPNRCTLPEV TFTPSKFASS HTPSRAEDQD NMEPTDPDPF LSVDMDNMRS
RTPRRGSLAP PVPETPPPDE QTGPRTRSRS QTPTPSRPIH AMTPPDSTFR PKRAKIFQRR
PSKKSEGVLP DGVLILIFSY LDIYQLMRLR SVSLHWSKIL TTSPDVCNNL DLSIYNRTVT
NKALIDVIIP FVGKRALSID ISNCFHLTDE GFSALSSLCG RGVHAWKMKS VWDISANAVL
EMANNAKEME EIDLSNCRKV SDNLLARIVG WVVTEPTLAQ QQNAARYKQH YALIPPVGTV
VGCPKLKRLT LSYCKHVTDR SMAHLAVHAH QRLQSMDLTR CTTITDGGFQ HWSIYKFAKL
EKLILADCTY LTDNAIVYLT NAAKGLKELD LSFCCALSDT ATEVLSLGCP QLRSLKLAFC
GSAVSDSSLR SIGLHLLELK ELSVRGCVRV TGIGVEAVVE GCTILEKFDV SQCKNLQKWL
DAGGEERSRR MYGRRGLKFE TKKGNGTLR
//
