ID F2PY66_TRIEC Unreviewed; 1122 AA.
AC F2PY66;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=EF hand domain-containing protein {ECO:0000313|EMBL:EGE06834.1};
GN ORFNames=TEQG_05889 {ECO:0000313|EMBL:EGE06834.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
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).
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DR EMBL; DS995752; EGE06834.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PY66; -.
DR VEuPathDB; FungiDB:TEQG_05889; -.
DR eggNOG; KOG0044; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_009681_0_0_1; -.
DR Proteomes; UP000009169; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd02340; ZZ_NBR1_like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR23055; CALCIUM BINDING PROTEINS; 1.
DR PANTHER; PTHR23055:SF178; RECOVERIN FAMILY PROTEIN DDB_G0274781; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..339
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 424..459
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 460..495
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 52..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 126368 MW; B0634F6B9698493B CRC64;
MSSSNAPSAI DGTSALTYRR TFFIVAAFAG TLALTQLHRY FFSSPAASQT LHRRNAVRHQ
RHSQRRGGIS LPSGETYESS SPLAPSLALA QREREGRSYG HFTLRVDAEH TLQCSLLPSQ
LASVETIQRE IGASLESANL MRHMIEEEFL TRFLIAEFPP SHVILLSTGE WRYLLNELTS
RGISELAVND AFTRFNENPH FGEQPDTERP VGQEDTNLVV NTSVTPAEQP PPPPPQPEIG
DTTIDDQSLF SWRDGTNDTA PPREGQNLLN LLYHIAEDQA RRDGYIHRGV TCNSCGVMPI
QGIRYRCANC IDYDLCETCE ASQVHILTHL FYKVRIPTPS LGSVKQVQPV LYPGKPNMLP
QTLPRNVAKR LKKETNFENT EVDALWDQFR CLANVEWPEE PNGLPMAIDR KTFDRCFIPN
RPPPPSLIYD RMFSFYDTNG DGLIGFEEFL KGLASFGNKS MHERLRRIFA AYDIDRDGYV
ERKDFLRIFR AYYTLSRDLT RDMMSGIEDD FMESGSRDVV LGSQPISAAF PGTIPGSDQS
RAGEGKRTNL QGDLEVIDNE AVVREDGDET GDRDIVLGDA ALRDTLGPNR HRQRDPSRSD
STTQGPYYGP RPSDSSADHG DGFDLICAGP YPCENFLNWP PAEHVQREDI INALGAYVPL
EDVTDFVDRA RIGTCLIERL NAAEAEHQSN IRREGIEERW RRRAFYLEEE EGTSGRPMYK
GNEDDYEATA SDGECNEDSD WHNPTPRSRS SSKVRFQDDV TDNEYETRSN QSTSSRSIQL
GERWGGYEIP EVERDAGKEI LYQVTQQGLN ELLDLIFKPK EDLLMEAYRT RTERKRWAKE
IERFQERGYR VKDIKNCDRR NPNGDDTDDP ESAGNKSLKD LLQESGFSVD PEFLEEVERE
EDGLDQAYSS QQEGSVISDH LSDHEVDYMP IASESNNFQG DTESPSSSEN NIPLPPDPTL
PQNRPNEEDL VALEHLPHGA HHSPRPHSAE PHPIYESAST STSASGPSHR HLSSQRRPRN
RSLPLRLRFQ QSPPPNRTRS NSGSSVASSS SAPSVKNAVL PSPPPSPKIL SRWAKLNLAE
QEAKERGGSG AKLNFEEFAR RMQGERGKRL GFVASWIDMT TF
//
