ID A0A3F3QII1_9EURO Unreviewed; 1156 AA.
AC A0A3F3QII1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=EF hand domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDQ94DRAFT_176801 {ECO:0000313|EMBL:RDH39073.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH39073.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH39073.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH39073.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ852032; RDH39073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3QII1; -.
DR STRING; 1341132.A0A3F3QII1; -.
DR OrthoDB; 1329809at2759; -.
DR Proteomes; UP000253729; 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; 2.
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 PRINTS; PR00450; RECOVERIN.
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 Reference proteome {ECO:0000313|Proteomes:UP000253729};
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 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..328
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 416..451
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 452..487
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 41..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 129578 MW; F77B8EBC0EFFCED8 CRC64;
MSDTRPRLAL SRYRPILYLL SGVAAAYAIV YIHNYIISSP PSPSRTSLRR RRAVRRRRRR
SEASNASDHP VDDTPSTRAI AHLEQLERQN GVYGTFRIET EDGRRVESGL LPSLLATRDQ
LMEEVGVPQA HAERMREMME DTFLESFLAL DFPPTHFIQE GCPEWEYLMV ELQRRGISQA
GIERALMRFN ADNNYGEELR RRRQNGERVT LSTSTFPEES PPVPNMDGGE TVVDDQSVFS
WRDGNNDSSP TREGQNLLNL LYHIAEDQAR RDGYIHRGVT CNSCGAMPIQ GIRYRCANCI
DYDLCETCEA MGVHIKTHLF YKVRIPAPFL GNPRQSQPVW YPGKPTMLPR SLSRSLAKRL
MKETSLENTE LDALWDQFRC LANHEWEEDP NKLYMAIDRK TFDRCFVPNT SIRPPPPSLI
YDRMFAFYDT NGDGLIGFEE FLKGIASLNN KSNDERLRRV FIGYDIDGDG YIERKDFLRV
FRAYYALSRE LTRDMVAGME DDFLEGGARD VVLGSQPISS AFPGSIPSGE ASRTGEGKRM
NQDGDMELVD NEGIVRSDRA DTADRHSVVG DAAVRSQYGS VRPMFPTAAR LATPSGSGVA
HTSGSNTRRE VNGDDGSNIP DDASNSSGAS DRWPPPEHVR DYDIVNALGY HVPLNDITDP
ADRARVGTAV YNRMCAQDRI RVNVTRSTGI HNRWQRRRFY TDEEDGATAP PGYRSDMDVD
GLSEDEDEDD VDEPQPDSHP PSPRSRSSSK VRFQDDLTDD YDVRSNPSTS SRSILVGERW
GGFEIPEVER DVGKEILYQV TQQGFNELLD LLFKPKEDLL MEAFRTRAER KMWAREIEQV
EQMESGTQLG PEEGRQTNDE PGEPPESTMV NPFRDHSLDE LLSRAGYSVR SPPLEPVQDG
PVLPPPTPDL GVPNDDVVYL GVPEVEEEGD DEESMDPRTS HDFLRTLGTQ HTPMSPSSHA
STFEEDDEVV DDDDDEEASR PPSTASYYDP TLPHHRPNEP GEHDHDDSDL ILSSSTNSPP
TSPSHLAFHP QQSHHLPAEL RLEPTATTSF PAPTSPSISS PEAEATAPKL SPSPIHPLPL
SSSSSAPPLA RQASPPRPPS KARIAHLAYL EKVEREAKER GGSGAKLNFS EFAQRMAMDR
GRALAFVASW IEMASF
//
