ID F2SZH0_TRIRC Unreviewed; 2108 AA.
AC F2SZH0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=TERG_07942 {ECO:0000313|EMBL:EGD91722.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD91722.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
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DR EMBL; GG700658; EGD91722.1; -; Genomic_DNA.
DR RefSeq; XP_003231641.1; XM_003231593.1.
DR STRING; 559305.F2SZH0; -.
DR GeneID; 10371406; -.
DR VEuPathDB; FungiDB:TERG_07942; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; F2SZH0; -.
DR OMA; TLFIAWN; -.
DR OrthoDB; 1386981at2759; -.
DR Proteomes; UP000008864; 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:UP000008864};
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 359..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 827..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 850..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 962..985
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1189..1216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1236..1257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1269..1287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1329..1348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1394..1412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1443..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1523..1543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1555..1573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1585..1605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1611..1629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1641..1665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1741..1760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1779..1814
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..2001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2031..2055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2108 AA; 237860 MW; 0F886BF6F8146526 CRC64;
MAPSENPSYD ANNQSGSHSI PLQDLSRPPG TVIADGAGRR ARSATIEDEL PGRQTSVRGI
RAIGRPLSQR YERIAENSPT GDRRADDPDN FESVSLSNDA GPSGFDHASF HQSTIGLSFG
PQQVRHSGSS MVRRSDDNSY FGASEDTVGQ TGSGSFVGEN DSLPLTDSRY LQPISGASVP
DAQAQVKRNS NEDRSVHFAG SAMGGGSHLG DDLESGLRSG RSSVRNSHRS ATGRLSPSPS
PSSALSRASS MMRMVSQRVV NLSNEPEVIE SVMRQKSVLK HARLDEPPSL PAMFEYAHDV
ASSETVNEGG QEKRSSKPKR KHGHPAISPL RGKALGIFSA DNPVRRWLCE LLVHPATEPI
ILILIIIQTI LLAIESSVHT GRKGSWSSPV VDILFLAIFI IYTLELIART IVSGFILNPE
EYSTLDRSAG FRNAVMIKAR ELFSLQRQPS TKKPADPQQM SIIRSFTTMQ QQADEVGDSR
QQQRIRLARR AFLRHSFNRL DFLAVVSYWI AFALSVLSID TNHHIYIFKM LSSLRILRLL
ALTSGTTVIL RSLKKAAPLL VNVAFFICFF WLLFAIIGIQ SFKSSLRRTC VWVDPLGVSN
FTFNQAPDTV QFCGGHLDNI TGLAKPWIHA NGQNGTTSPK GHLCPQGSLC IEGSNPYAGT
MSFDDVLHSL ELVFVIMSSN TFSDLLYFTT DSDYLAASLF FIAGFIFLSL WLVNLLVAVI
TSSFQVIREE SKRSAFTADR IDDVGPEDTS FRRVSKLKRL FNRTNYVWIG IIAFGLIVQC
LRSSSMSSNR KELIDSTESA VTVILFIEIC FRIGVDWRNF FKSRQNWADL ILAIITMVMQ
IPPIRSSGGV YAALSIFQVL RVYRIVLAFS LTRTLIMTVF SNIVGLFNLI IFVFLITFLT
SIFAVQLFRD QIPAMDSDGE VTRTTFSNIY NSFLGMYQIL SSENWTSILY SATEANSPRG
TAWISAAFFI MWFVLANFVV LNMFIAVIQE SFDISEDEKR LYQVRAFLQQ KQLSESSHGN
LALSSIFKLG RGRERYRDPL DHGPAALEML LKEAVVQDFL DETSPLRPME TQPTEHPPEQ
QAVQPGFFSR IFNKLTERVL NREPNPFYSK LKFSRDHDEL DPAAMAKEVL SAAEQRKRAQ
RQYLQRYPKY NVSLYIFTPS NPIRRICQRM VGPGRGKSRI EGVDPYKPVW YLFSAFIYAA
IVSMVLIACI CTPLYQRAYF ETHGPGIHNW FVWTDLWFAI LFSVEAVIKV IADGFFWTPN
AYFRGSWGFI DGIVLITLWV NVVAALYRTG DVSRVVGAFR ALRALRLLNV SESARETFHS
VIVMGGWKVI SAAFVSMSFL IPFAIYGLNL FNGQMKQCND GDFGYVSLAH CVGEYKSSQF
QWQVLAPRAV HNPFYSFDNF GSSLFILFQI VSQEGWTDVL WNAMSITGVN KQPQPFSSQA
NGLFFVVFNL LGAVFVLTLF VSVFMRNYTE QTGVAFLTAE QRSWLELRKL LKQISPSKRS
LNKGNNKFKA WCYRVAVKKH GRWARFITGL LLVHLVLLVL EFYPEVDWWE RTRDALFLFL
TLFYIANVVI RLVGLTWPRF RRSSWDLYSI LSVVGTFITT LLALINDKSI VFAQLHKLFL
VSIALLIIPR NNQLDQLFKT AAASLTSIGN LLATWFILFL VYAIALTQIF GLTKFGGSET
SNLNFRSVPK ALILLFRMSC GEGWNQIMED FATMEPPYCT LGENFYRSDC GSAAWARTLL
ISWNILSMYI FVSLFVSLIF ESFSYVYQRS SGLYAISRDE IRRFKQAWST FDPDGTGYIS
KEAFPRLLGE LSGVFEMRIY EGDFTVGRIL EDCRVNVRES ELSHSRSVGE LDLKKLMLRL
SHLPVAEIRK RRARLNAFYE EVLVSADPER GISFTSCLMI LAHYNVITDS KSLRLEEFLR
RRARLQRVEE AVRRNVVVGF FNTLYWSRRF RQRIQARHDS RLVSVPQFSV PEIYVEDEDG
LMDEDQSRRA SEDRARSPEG SPSRKAPRIA LPKIETNMFG DEAHRLPSPT HSDWGNFNPS
LTPQSPTTTY DSSMPRDESG EGHGHQRGDS SVSVQNVQDV LDSFDHSVWG ESIRRSFTRR
RSHGSAGE
//
