ID A0A0V0QMJ2_PSEPJ Unreviewed; 2595 AA.
AC A0A0V0QMJ2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Ion transport domain-containing protein {ECO:0000259|Pfam:PF00520};
GN ORFNames=PPERSA_12681 {ECO:0000313|EMBL:KRX03551.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03551.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03551.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03551.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX03551.1}.
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DR EMBL; LDAU01000130; KRX03551.1; -; Genomic_DNA.
DR EnsemblProtists; KRX03551; KRX03551; PPERSA_12681.
DR InParanoid; A0A0V0QMJ2; -.
DR OMA; CITRINI; -.
DR OrthoDB; 180975at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF7; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602077-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2595
FT /note="Ion transport domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006867519"
FT TRANSMEM 110..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1180..1201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1213..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1262..1288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1348..1371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1575..1594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1614..1635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1709..1731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1833..1860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1904..1927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1947..1967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1979..1997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2049..2068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2119..2142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..141
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1145..1381
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1573..1861
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1913..2146
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 258..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2314..2335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2353..2406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2474..2507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2526..2560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2572..2595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2370
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1792
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2595 AA; 302881 MW; E0FB3D77BB7085F9 CRC64;
MLMFFFMIFA IAGLQLFQGV LYKRCYYEET GIIADTNDGT EPYCNDDGDC NQWEEGDLGQ
LICGKMGANP DWGQTNFDSF PQSLMQVFII VTLEGWSDIM YSVMKTYQSW VVIFFIVIVF
VGAFFLMNLT LAIIKVKYKD AQTEPIQDST KKDMVRGYGL KKLIQGNIYE SKKLNIHIED
IKWVGNQNQE EDFQTDRNLK DKISKLTKLK GTTLDSERDG DDRQQGLIRD FNKNTTIIIE
NTTPQDNSYI NKDINPRKLQ KQRSSKIKDQ KSGVQEDDKQ NKNMEVLDMI KRARRKSTTR
QTVVQRLIEP KKSIYEASST ILLQRRNKQF QRPGVSRFQG IGVSSQKKHT QVLTDLQKQK
LRSMIQKHKQ VHYRHSNLEN KKVLKPSFVQ ANDRKMLMAG PVVNFQRQIK QKKQENQIKE
NSQAILQSGN IGYLTKRSSQ LSSSRMQQSY KDNHSSDYNN MLKSSQNNLQ SDEEENEEEI
DIEQLKAQNN QEVPQHKYED QFKVNIMKLR KKQIQSQKKQ KQKQRQQREN SIKVRENKYI
KQNQLTPQNQ NQQASKSLQL SKNVNTQQSD NKEKSEIKIY IDNVKMEQSK NVRKNQNKSS
SQSFSKQQEK ILNNQLANSN YKSQHSKTYL MNKSNASYQG IKQQSQLQSK QTDQANQINN
LSITLSLPST FRSISSDNDD NEDHSFDIHN PRNRLILQDD EDFTAEQQFN HKFHQDIEAI
REDKYIIEKK KRIMAAEQKK RKTILMDKKK PASQKQHQNL RKINFIEDED EEIARLRIIL
KPRYLKTRIS YTIDKQQDEQ INDVMPSKIQ NQKKLLEEEQ NEIKKQLKFK IKYEFEQPRI
REIAIKRKNQ GSKFFFAQSG QQTISYINKS VSPSSQQWYR QNRKSNGHSS LQNSSNPGSP
VQNTDNNNIV YDSLGNQIYQ QKSIVQNTHN QYSFYSFNSK READKKIGRL EANMMSKIDK
FFIQNKYFLN EDNNQLQTQQ TQENQNDPNG NSQQKKQNSV YSNQKSVQSD DQSDTQENNK
DKKEKNKNKN EDKEKDNEDD LDELALYNKE EDELIKMYDK IVNDMFTTRQ LNENGLQNLD
VKWSGEDVNG VPPNFLAKNY SLVQRMDNII KSLNYSIFDY EMWEGGLFGI IQSIRRIVLK
IVLNKCYDYL IMICVLLNTL ILAMNGLVSV KGQATLDNYN YIFTIVFTVD MGLKLIGMGV
MDYVRDQMNI FDGVIVLLSW VEFSLLNGSN STFSAFRSVR ILRTFRVLRV TKLIRSLRYM
QIIVEVIGNT LSSFFYIFLL MFLFNYIYAL LGMQQFDDKF DFDDSPTRMS FNTFLDSFMA
VFQVMSMENW NDILHACLRT DNPQYLTLIF LISWIFIGNY VLLNLFLSIL LDAFDDQAQK
NQDDLKFEIA QDLAFSSAES LTSSYFLSGS SKLKSQMQSQ LQSQSANNKH LNQVAPQSFQ
NSPSQLNAQS KFIMPLMINN QQIMSPQLKQ SQNSNLGSNN NFGQNNLLVK AAQNDIQDEE
GMLQSQDNGQ KTVLSSLANQ EDDEATLEKS NQKKNNKLKK ELVMFENIKC ERAFYFISKQ
NCIRRFCYRI VKHEYFESVI LGAIVLSSVK LAVDTYTDTL DNTMITNLGT NLDLVFNIFF
LLESIFKAIS FGFVIDENSY LRESWSQLDF LIVLINIVDT IFQYSSFKSL NLGFVKILRL
LRILRPLRFI SHNKNMKIVV TALMESAPAV INVLIVVLLI WLMFAILGIS FMQGRLYRCV
FPESMEVDDD YIYEVDMDAC NDIEGASWER YNLNFDNIFT GMLTLFVLAT QEGWPDYMWY
FVDGSDTVTD YDSPYYGKNI QPPIKNNLPL FQIYFIVFLF IGSWFLLNLF IGVVQLNFIL
AESAAKNKFL SDDQAKWIEI QRLIVKSRLD FASVKPPNNK YRQIIWNFCQ SWVLDTIVMT
CIILNIITMA MSYEGMSTGY ETVLSNINLA FTSVFILECI LKLTAYGLRG YFYNKWNQFD
FFVVCTSIID LIMFNFLESS IEVLAVGPQL GRVFRVLRVT RLFRLIKAFQ DLKQLIQVTI
LTLPQLMNIS ALLFLVFFIF SILGNTLFSE ITNGEIINEY MNFSNFHKAF ILLLQCSTGE
DWFAAMFTTM NEVSQWSWIY FVVFVILIQF IMINLFILVI LVQFEENFIT VGEDNPLMAF
QDNESSFKAL WIKYTRSERG IKMHQNKLTD FFLDLEEPLG LDWKNKKINY IENIKIHHKD
LTNSDLEQLI ASERVRLYKQ ASQLLMHMQI NTDHEGYIYY NDLLFFFYKD FLKEKTEAIV
PKSQFESEVE TINNYNEALK LIEQEEKKSE RTMTKLKRKQ NKNYKQRGHN LPQANPMERI
LFGSNFIPEV LTSTENSSDD ESDDDFSNDD FSGDNENKVI DENDEYESQR SIKKKQKKNK
KNIKKREHGV AKAININIRK FKDINKINTD IYQQEIDYEY DVEQDSLNPS NILLEGMSRR
GSHMSRQSNL YFNKDSTQKQ KLSKQQSINS QQKTPMNNNT NKRNSNFSSQ LDRNFLNIQS
SQFRNNTYNY GGNNNNSHKN ITGSHKNIPY NSPQYSDQDT VNNNYYSSKN KLLLRGDDKN
SSEQQSDGEL KAQEK
//
