ID A0A150VER0_9PEZI Unreviewed; 2247 AA.
AC A0A150VER0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=M433DRAFT_150469 {ECO:0000313|EMBL:KYG49026.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49026.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG49026.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG49026.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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:KYG49026.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPDO01000033; KYG49026.1; -; Genomic_DNA.
DR STRING; 766039.A0A150VER0; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; 5.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
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 TRANSMEM 404..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 956..977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1061
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1265..1292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1312..1333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1345..1363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1405..1428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1478..1496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1527..1549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1609..1629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1641..1661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1673..1694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1727..1752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1821..1846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1865..1900
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2218..2247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2233..2247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2247 AA; 253533 MW; B9DD62383D3BA305 CRC64;
MESEEDSAHR RNQSFNAIPL QDLDSNGTSH HNGLDVESGV SHRRTLSDRG RTLFNRGRER
DRAQNTQRYS PIGERSPSPP QSALPPRGAP LSPIAYVTSP SGQHERIPDE DDETEPLSPV
ADRGAFQAAI GFAGLSFNED HMPSDHEEDD AVQQTPPQKR RMSRSSLPTL RTMRSQDEEM
VSIQLDDGPA FFSPIGAADE DDTQPLTDSS HVRPSTLAAP STPHGQRHDR QRIRENSNLS
VRFLPGRGRS SSRLGDDLPN LEMGAYSSSS GLSPTSSLRQ NSPSLSASES PLQRTGTMLR
KMSQRVVNVS NESDMIERSI KRKSSMSRGT VPPVPSLSRS MSESGNASMD GSAPRSPASE
KIPSPKIESA MLHQLPAIDR NPLRGRALGI FPPESPLRRR LLSLLVHPLF EPFILLLIIL
QTIILAVDSA SNVYDHPRPS SWGGPWTDWV LLIIFIIYTI EIGIKMVVSG FIFNPREYST
IDRSIGLRQA LAKKANDLFA LHRKPSIRGQ IDDQIEAQGP PSLLRTFTAQ TLEDEIPGGS
RQAQKKRLAH RAFLRHSFNR LDFVAVAAFW ISFVLTIFKE ESRFHIYVFR MLSCLRILRL
LGITSGTSVI LRSLKRAAPT LLNIGFLICF FWLLFAIVGV QSFKSSLRRT CIWNWQNMSD
PSQGEYVSDN VTLFQFCGGW IAENGSTMPW LTADGAWGAN EPKGYWCPQG SWCVEGENPY
NGTVSFDNIL NSAELVFVIM TSNTFTDLMY YTMNSDYMAA ALYFAAGIVI LTLWLISLLI
AVITSSFQVI REESMTSAFT AEEFDPADDN TRKQEEDKTS SKHRRRIAGL RRWYEKTRWF
WIIVIIYGLV AQCFRSAYNS NGTKQFMYVS ELGVTLALLV EIIIRFAADW RDFFHHRQNW
VDLGLAIITT IIQIPEIRYS GQLYAWLTIF QILRIYRVVL AVKITRDLIT LVLRHVSGIL
NLILFVFLLT FLAAIFASQL FRGEIPAQDN QGNTIEVTFA DIYNSFLGMY QILSSENWTQ
IVYDVTRFTT HYGTAWIGAA FFILWFTLSC FIVLNMFIAV IQENFDVSED QKRLQQVRMF
LQQKELGSNS SGTLSLSTIF KFGHAKRQDP LDFGSAASEQ LLKDAVVRDF LDEQMKDANG
DGGGPGSGVH HAATDIVQES SNWLEKARDW VANRFFNREA NPFYSRLQLT KAYDQLDPQT
LAREVYNATE QRKITQREYL RRYPTYNNSL YIFSPENKIR RLCQRIVGPG RGSERAQGLD
PNPTVWYCFS AFIYAAIVAM VLLACITTPL YQKEYFEKHG FSADNWFVFS DMGFAALFTV
EAIIKVIADG FFWTPNAYFR SSWGFIDGVV LITIWINVIM LLTDPTGGSR TIGAFKALRA
LRLLNVSDSA RDTFHSVIIL GGWKVISAAF VSISLLIPFA IYGVNLFAGQ FSHCNDMIPN
SGPPMGPGDV ANLTDCVGEY QSSPFAWNVL APRVATNYYY NFDSFSSSLF ILFQIVSQEG
WIDVMNSAEA ITGIWTQPSA FSSPGNAVFF VVFNLLGTVF VLTLFVSVFM RNYTEQTGVA
FLTAEQRSWL ELRKLLRQVA PSKRPNTKKK REGWQEWCYR RAVTKTGRWQ RAMTLVLVAH
LVLLCLEWYP DNSPWPKIRD IIFLLFTIFY IANIIIRIVG LSWTRFRKSA WDVYSLFAVS
GSFITIILML TNFASRDYTQ ANKLFLVSIA LLLIPRNNQL DQLFKTAAAS FTAIANLLAT
WFVLFLVFAI ALTQTFGLTR FATNETVNLN FRTVPKALIF LFRTSMGEGW NQLMQDYASV
FPPRCVVGST YYNGDCGSSQ WAHALFITWN ILSMYIFVNL FISLIYESFS YVYQRSSGLS
VISREEIRRF KQAWAEFDPN GTGYITKEMF PRFLGELSGV FEMRIYDGDF SVRTLVEDCK
IKRQSSSRTS LLPIDGSSVG SYEIDIEKLN RRLAELPVEQ IRARRARMNH FFEEVLVSAD
PDRGISFNGL LMILAHYKVI NDNKSLKLEE FLRRRARLQR VQEAVNRNIV IGFFDTLYWR
RFFRRHRDAK QNARITAIPR LGVPEIFVHD DDAPQNVSHV KMMDVPSVSV TPVELEPSDP
ADGIGVGRAP ASGSDYGSHR STGAETVMRN RSGSIQHSEP DSDLPPPRGS PTLFASHGPS
PSASSIQPDW HFAAAMENAV QAVSPPPSPS LMPEANVAAR SRSNSAVSSN EEIMRGMFQD
SAWGQSMRRS FTTKRGSGEK DARRPSS
//
