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Database: UniProt
Entry: A0A2T4BZ71_TRILO
LinkDB: A0A2T4BZ71_TRILO
Original site: A0A2T4BZ71_TRILO 
ID   A0A2T4BZ71_TRILO        Unreviewed;       785 AA.
AC   A0A2T4BZ71;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=EF-hand {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M440DRAFT_1358756 {ECO:0000313|EMBL:PTB74535.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB74535.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB74535.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB74535.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ679135; PTB74535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4BZ71; -.
DR   STRING; 983965.A0A2T4BZ71; -.
DR   Proteomes; UP000240760; Unassembled WGS sequence.
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; 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; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240760};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          1..43
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          163..198
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          338..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..375
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..720
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  89277 MW;  28F0E3038882E732 CRC64;
     MVPIRGVRYR CANCADFDLC ETCESQGVHI KTHIFYKIRI PAPPFGPRQM QPVWYTGDPD
     SCRRNLPRAL ITKLTRETGF ERPELEAFWE QWTFMANTEW RDDPSELGIA MDRKTFERCL
     VPTGGSRHAS PNLIHDRMFA FYDDNKDDLI GFSEFLRGLS YRKRKDKLRK VFDGYDLDGD
     GFVDRRDFLR MFRAYYVLYK QMHKDILDGL EDQLLASSEA QQLVASRQPL SSLFGREGRV
     PTADGPLAFS GKTLYPDGHV EIDVGMEDAV VPDTSDTADR DEILTNLFAY DTDPYSRRRM
     PPADDVDTNW RTVRTLTSND VDRAYFLALM QPPASLEELP GAITGNNGLD DNATDNATDE
     TSDDDATEDK EADEDNDHAD SSSSQRHDFT SVFRTTDRIP TESEIRASYV NHYRQHGPRM
     TRRRQDLARR QLHERWKRRH FYLDEEEGGE PPSQWEEEED ILETSGIMGE NSKRASPHVA
     STHSRSSSKA RLAEDTSDLE TQSDTSASFA SQPERWAGLG IPVAEKDAGK EILYQVTQQA
     FNELLDIIFK QAEDLAVQAA ATKEQRVKYK AEIDAVSLAD DKMEDGNGGQ QEDVSLYAEK
     SPRHKTLEEL LEESGYMLDS SQQEPRNAVE ISIVEEIIRE EHALEAGEQS SNPAEGETTE
     SEPESLDEAE DEHRDPTLPQ FRPNSVPVTS PPPPPSSSKR KEKEPSKDGS KTEAEKPPAS
     KKISSEPSIK TLRRWKKLNM AEQQAAERGG WGRLNFAEFE EIYKNQEHQG NRLDYLGSWI
     DFCIP
//
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