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Database: UniProt
Entry: A0A178B8J5_9PLEO
LinkDB: A0A178B8J5_9PLEO
Original site: A0A178B8J5_9PLEO 
ID   A0A178B8J5_9PLEO        Unreviewed;       957 AA.
AC   A0A178B8J5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=EF-hand {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IQ06DRAFT_323054 {ECO:0000313|EMBL:OAL05882.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL05882.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL05882.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL05882.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441706; OAL05882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178B8J5; -.
DR   STRING; 765868.A0A178B8J5; -.
DR   InParanoid; A0A178B8J5; -.
DR   OrthoDB; 1329809at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 3.
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; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          159..211
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          297..332
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          333..368
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          502..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  109001 MW;  266DF0158CA8742E CRC64;
     MSLSPYTATR IPLNPHNLIS RSELRELITQ QVPELTPEHI DQDIEYVYDV FLDRLLAMVT
     PNRPPSQIET EAIARWVAER HGDRISQPNM AVERAAARHT AMLENATLPG LDGAESIAGT
     DLWSDDATED GANHPDGQTL QRTLYHIAED RARHEGVVHR GITCNGCDEK PIRGVRWRCA
     NCSDYDLCSN CEATNSHIKT HVFVKIRVPA PYFGTIKQEP LYPGKPHVMS SSVPSALKKR
     LLSETKMEAE EVDALWDQFT CLASTEWTND PNSIGWALDR KAFDYAFVPR FKNFVAAPNL
     VYDRIFAYYD SDRNSLIGFE EWIKGIDGMH ATNGHVKSKI VFNGYDIDGD GFISRKDVLR
     IFRAYYALEN EGTRNYVANI TEELMTRNAL DTVNSSQPLG SAFAPHGLAA NESENPRLSE
     KNQDDFEITE PVLQENQQDI AERDEMLKMA NIRNIGSELL PQSEQDLIVT NRWGRREFYT
     DQEEGFAQPE GMNDDTALEE NDRITPSSEN EEHEDALPPR SSRPRWSRSS SRVRFQDDVD
     IETRSNASTS SRPFGERWGG YEIPEPEKDL GKEVLYQITQ EAFNELLDPL FEDRENNAMD
     AHATRSERRQ CAAKLEQITE RFRKEDSLFL DAICRIGIFR YTKCVTDMLC NAVNETLHKD
     LNGTHRDFRN PESGTFDRDS TRTILTDLYD RVHRTFADTV AIADDEPKAS DMALWNTWLC
     QQRFQQELLD ALIEPVMIIA GAKTQRTQDQ QVTEPVHRDP TMPQFRPNST ADLFAAELAK
     ADIKASHEAH PPEDSPLRSS SAGPFFVCTS PENESHSPET EQVEESENTV PLTKSPLPDW
     KLVNWRDYTD NPMIHAVQIH TSNGTSYLRA STKPIIHSSH SFEPAFDQLR PLHRHVRELA
     MDPTSESHLI LLASLEAVQQ EIRERGGSGL INFDEFDELM REGNLRFLES WMEWVSI
//
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