ID A3LZH5_PICST Unreviewed; 868 AA.
AC A3LZH5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Leucine rich repeat protein, contains F-box {ECO:0000313|EMBL:ABN68338.2};
DE Flags: Fragment;
GN Name=FBX1 {ECO:0000313|EMBL:ABN68338.2};
GN ORFNames=PICST_63653 {ECO:0000313|EMBL:ABN68338.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68338.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68338.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000501; ABN68338.2; -; Genomic_DNA.
DR RefSeq; XP_001386367.2; XM_001386330.1.
DR AlphaFoldDB; A3LZH5; -.
DR STRING; 322104.A3LZH5; -.
DR GeneID; 4840674; -.
DR KEGG; pic:PICST_63653; -.
DR eggNOG; KOG0498; Eukaryota.
DR eggNOG; KOG0500; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_006113_0_0_1; -.
DR InParanoid; A3LZH5; -.
DR OMA; RMKSVWD; -.
DR OrthoDB; 1330350at2759; -.
DR Proteomes; UP000002258; Chromosome 7.
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; 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; PF12937; F-box-like; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00256; FBOX; 1.
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:UP000002258};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 26..143
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 194..307
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 477..524
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABN68338.2"
SQ SEQUENCE 868 AA; 97118 MW; A2454A0011046198 CRC64;
DNTKNSNNAN GNVPPDFFNR LQTFPLFNKA PKSFHTKVAS KLTLMQYHPQ EYIIKKGDPS
KSMYWILKGT VSVTSTDGES IYAELAAGSF FGEIGILFNR PRTATVVART KVLVGVLTSD
ALNTVLKHYP LIERRIRDEA QERLAMQDKK NKYDLPNLIS NKMIESAPSL PPIRNGINAN
ATISIQDFIK NLPIFQNLPS TIIHQLALGV EPINFNAFEY IIHKGDTNSD IYFIINGEVE
VIDYSRNQEG AHIERILARL SSGSYFGEMS FLSFLNDKHS DCVRSASIRS ISTVELMVVK
SDKLEDLCEK YPFIVDDMRK TAEERNKLNN SINSKGSEHD NKTRLSIDYI IHKQDKDRSD
EEESSHDTSE KSSPEKSPSS QPNLQHPQSQ RVGSPSVSPI SSDAKMSTST RNTSFADEPF
SRKRKSVSNI VPSVNYFQNF QFANSTSNRN AFQYMPHNKR IRLASISGTG RRRSSILSNN
GPLPDRILLR VFEFLSLPEL MKLRIISRRW RQLLSVASNL CTNLDLTPWN TSIDDQALIS
ITDFVGTRPQ QINISNCFHI TDEGFSYMVN EIGISGNIKV LKMKSNWEVS AMAIMDLTVP
SVGGYLEEID LSNCRKVRDI VLERLLGWDS SAIKEELSQQ QNINGSSPEI DHDLDQIGCK
SLKILNIGYC KHLTDNVMQH IANHASQRLE SLDLTRCTAI TDRGFQYWTY KSFPNLKKLS
LKDCTFLTDK SIISIANSAT NLEILDLNFC CALSDIAIEV LCLGCPNIRE LDLSFCGSAV
SDSSLVAISL HLRSLEKLIL KGCVRVTRAG VDALLSGCSP LSYINISQCK NAHIYPGNIP
AQKLNVNPQT KSAFVTAGSN QNIIEIVI
//
