ID F0W467_9STRA Unreviewed; 2027 AA.
AC F0W467;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN Name=AlNc14C16G1748 {ECO:0000313|EMBL:CCA15870.1};
GN ORFNames=ALNC14_020130 {ECO:0000313|EMBL:CCA15870.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA15870.1};
RN [1] {ECO:0000313|EMBL:CCA15870.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA15870.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000256|RuleBase:RU361221}.
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DR EMBL; FR824061; CCA15870.1; -; Genomic_DNA.
DR EnsemblProtists; CCA15870; CCA15870; ALNC14_020130.
DR HOGENOM; CLU_001605_0_0_1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd01867; Rab8_Rab10_Rab13_like; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11689; CHLORIDE CHANNEL PROTEIN CLC FAMILY MEMBER; 1.
DR PANTHER; PTHR11689:SF136; H(+)_CL(-) EXCHANGE TRANSPORTER 6; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Chloride {ECO:0000256|RuleBase:RU361221};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361221};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221}.
FT TRANSMEM 73..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 237..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 367..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 1067..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 1125..1145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 1194..1215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 1253..1272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 819..876
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 703..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2027 AA; 226912 MW; D0E81830081BB2EA CRC64;
MVRKASQLLG DAGKARSLTI HVSMFLSLRE THLIFRFIRK CCEQTCSHPT VWPGAKFMYT
AGQEQRRLVY VRWVVTLLTG MITSLVAVLL LFCTKYLISI KHKLLEAVVH AELNQSVFFG
CAFWALVGCN LAFVSIAAIL TSFWEPVAAG SGISEVKTML NGMKIPRMLR LRTCITKIVG
TIFAVSGGLP VGKEGPMIHS GAIVAAGLSQ GKSSTLGYDT SFTHFTAFRN DREKRDFAAC
GAAAGVAAAF GAPIGGVMFV LEEGASFWNQ TLTWRTLFCA MAATFTLAFF LSGMNDNLSW
GTLGSHTGSF TFGPFSSSTY QLWEVPVFIM MGIGGGLQGA LFNAINTRIA RLRSRWVNSS
RVAYMEAILV SLLVTSMSFA APFLFGECRP LPRNHDLSSI VQPGGLATSK AFTFAMESMR
RNTTACICES CVDIALDGAD CFHADETIEY PYKKELTRFY CPEGYYNDLA SLLLTSGEIA
IKHLFHAPPN AFSVQNLILF WSLMLGLACI TYGIKVPSGL FIPALLIGAA YGRLWTRVIN
FYSHWGHAKI VDPRAYGLVG SAAMLGGVTR MTISLTVIIL ECTGNVEYGL PLILTSFFAR
WVGNAFNEGI YDIHIHLRHV PFLDWNPPLP GSFLRVKHIM SPHPKCLYMI ERVGVIFDLL
TTTKHNAFPV VVEDPNFGKR FFAGIILRKQ LNVILRRQDF SAEKPQPFSR HPGSNPRSKP
FVHQSGPNQV EEGTPKEMKS PRDNLALLGS DHSPIRLDLD RNFPHGSCLS YDDMEVYYPR
YPIPVISIGM KAGMGVDDGE PYSIKEEDRQ QWVDLTPYMN QTPYLIQEDA PFTRAYRLFR
SMGLRHLVVV NRCNNVCGII TRRELEQEHC NRCYRLAQHG AIDDADTLYP AQQFVATWTE
YFVLAIMDPD GLFTRDSNDA DKASSLGKKG QHLDDMELGR KRRASTESLY PLSAISLKAF
LNSVEKGDKF TPRESDGIEQ IIFRTSHLPM QDSTFGRHGH QRTRRAAAGS FGAERRKGHG
MVSSRDKRFR VNGYVVDQDI RCGPKSGWTT VYQMMFQSNS PTGQRTALLL LIMVSISVTI
AILDSVESIR MQVGSVLLGL EFFFTLVFSA EYFSRVMCLQ KPQEYVLSLL GVIDLAALVP
TYLGFMMASS RPLIHLAVLR IFRVMKVFRI LRLGRFVDAA AALQDNIHHN KRRITVFLVG
LFTMILVIGC AMYLIEGGNT GFSNIPVSLY WTVVTITTVG YGDIAPTTIP GRLLATVVMF
AGYGFLACPL MLTQPSDSDV STEAIDCPRC LRRRESQKVR IISMVHSSSK YDLLIKLLLI
GDSGVGKSCV LLRYSDDSFT TSFITTIGID FKVKTIDVNG KRVKLQIWDT AGQERFRTIT
TAYYRGAMGI LMVYDVTDDH SFQNIRNWMT QIKQNASTNV NKILIGNKCD VDPSERAVTT
EQGQELADEF GIEFFETSAK SNINIDAAFH AIAVDIQKRL AESDQGRLDK RYLIESAMSS
SDSESWNDWV EDDEQEDCAS CDVLQCLFCT ETAPTIATFH AHLLASHEFS LQELFTRWKL
DHYAMIRLVN YIRSNSQKGL DPHSIWNKLD NNGVDEFADE IYFTPVLSND AVLYSLGDDD
EDSAKEDGNE TSHTEKSEST DLTSEHIQRL KAENLALRDQ ATITKAFIHK VTCGDEGNTD
KDLVTVSTQK KAKQVNFKVD ELDSYYFDSY SHVGIHYEML TDRVRTEAYR NAILNNAYLY
NDKVVLDVGC GTGILSMFAA QAGAAQVIGI DCSEFGHIAQ QIVEANGFTS KIQILKGRVE
DVKLPVDHVD IIISEWMGYC LFYESMLDTV LFARDKWLIS DKEGQLTGHV FPDSASLYLQ
GAQDPKYRKG FWENVYGFDM TAVQSKINTE NGFVEVVYPE AILTDRCLIY QVALDSVKTE
HLFSSTSEFE LRINRCGLFE GFVSSFDVSF TRDCLQAESL TTGVEGPPTH WQQVFFMIDS
PFNVRMDQII KGTWTLSRNA NNSRFLDIII TWVTPQGESF TQNFRIH
//
