ID A0A078AS51_STYLE Unreviewed; 1492 AA.
AC A0A078AS51;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Wd-40 repeat protein {ECO:0000313|EMBL:CDW84994.1};
GN Name=Contig5494.g5877 {ECO:0000313|EMBL:CDW84994.1};
GN ORFNames=STYLEM_14064 {ECO:0000313|EMBL:CDW84994.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW84994.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW84994.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW84994.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCKQ01013346; CDW84994.1; -; Genomic_DNA.
DR EnsemblProtists; CDW84994; CDW84994; STYLEM_14064.
DR InParanoid; A0A078AS51; -.
DR OrthoDB; 721380at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44019:SF8; POC1 CENTRIOLAR PROTEIN HOMOLOG; 1.
DR PANTHER; PTHR44019; WD REPEAT-CONTAINING PROTEIN 55; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT TRANSMEM 949..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1126..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 272..313
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 314..347
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 403..444
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1353..1388
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1453..1488
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 1492 AA; 173248 MW; 8D7F77F0C77C25C4 CRC64;
MTDKGLTEPL LNFKGLNNVL ASSSKPQTLP IDSEVNTVFA SIQTIGDKLV NGSEIEGRAK
HYIITRSGNL LNFSENGKLT LWSLLSKKLV YSEDVKRINV LYETPKGSKL FIGYNNGTLE
SRDPNTQQVL QQVNLRSAVK ALVSDDKNLY VSLKNGKILQ FSCKNISSVS QKVIRPIDRT
SPITHLKLSR DEIFLVGYVD IDQVEMLFVF NIIKPEQSWQ TKLDLSPGEL REDPDKLVVI
SEDCLNLFIR GENNKGVCMY SLFDGSVVQN VTSMHTNYIN QILITKDSKR VITCSKDRKI
KVWDWIKSEC LATLTLHEEG VETMVLSEDE TLLFTGSYDT AVNVWSMYDY VSLTKLKTQF
PIRSLHLSGD NDILLACGNL NSKTDQPMQA FWVLEDNADA FRIRVELKNV SNCYVTPNNE
YLVTMNGNSS LKIWNLKSRV LIEQHKVNCQ FRYNLRALNG TRDSESIFFQ KEQSEIIQWS
CSQQQQVHTF IHGSQVQDIV ITSDDRMMYC AIEKSIYKWD LQTKQELCRF LHPDGYFLYL
VLSSDDQRLL ANGLGADIFE YDLKLDDTQE LKRFDIIKDA CWLNFELSPD GVTLIQTHQY
NGSFWVCNLK EGRVVKILSK NSQIINFVGF TKDGKYLITR SESESIIWET SKWEALITIQ
EEFGVVTSSS RQVQAIIHDG LYKSWSDQIF CSFSDDFTFA SIEQEQEVEQ DVQEVNTSDI
KMTGKFNNLM KLFIGKVGKK SPDENKYLPY LYKTQIQPFK MTLAHFYAYF NRADIVQKLL
EMGSPYIEDV NQNTPLDYAI QKKSYESATI FLDYIIKSPN LYGKLTEEKI INLIEFAPSN
LKEFFDSAVK EQVGEYIPSF GTLITNPMSF RESQNNFVSF SDIKHMMVLD KDNDEPLVFK
TLQIPFNMQP GSQSSINLHR TLSQSELTAF RAESVQAILT YKWDLVKRIV YLNGLIYLFY
MAVLFTFIQT YHEISLYFLI AFGFYFMGFE ILQICLNRLS YLGDFWNIFD FLRVLLLIFF
IYNAFKHEDW NKSQSMLQLL GTLNFLSWVR ALSFLRLFQK TRIFIRLLVE VIYDMIPFMI
VLIGAVLGIS LSFEVINDIS MLEALKHNYR LTFGDFETDN YTAANWTLFI IGSVLIPLIM
LNMLVAIMSD TYARVMSDIL PSDFLELNQM ILEQEEIQFW NRRKGQLGYL HYVTPLKRKE
GNEWEGQIQK ILALLQQHNG QSPEVLNKLG EKMDLIMESQ KVQFRDTNLK FDEQKKRFDR
IQQELEIILP KSQKDEIVVE EEEDSDGDFF DDEYVEEQSK IAQTYFQINS CTVKKYLNGN
WLSFNPTKQG KLLKEESIKA IKQIFRRVNK KIPDESNIEN LMKEIDLNGD GLLSKIELYV
LFMRLWNYHQ EVEEEITLMN QSKYPKDAFS RFLESQQREI FEQLWTKYDS DNKDHIDAKQ
GTSLIKEFSK KSLNDQEIID LLKQLDRDGN GEISKDELKT FISENKYLLS EY
//