ID A0A0S4IQP1_BODSA Unreviewed; 1129 AA.
AC A0A0S4IQP1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Zinc finger protein, putative {ECO:0000313|EMBL:CUE73533.1};
GN ORFNames=BSAL_55255 {ECO:0000313|EMBL:CUE73533.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUE73533.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYKH01000153; CUE73533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4IQP1; -.
DR VEuPathDB; TriTrypDB:BSAL_55255; -.
DR OrthoDB; 1581354at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.2220; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13244; ZINC FINGER MYND DOMAIN CONTAINING PROTEIN 10; 1.
DR PANTHER; PTHR13244:SF7; ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 55..107
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 588..627
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 954..992
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 123124 MW; 4CC8D07A6FB58BA2 CRC64;
MPHTHKDRRM AQTPSAGSPT ASMLKLPQKK QTTGRPMSAG EDFFYTSEPQ SDLTCQVCLV
PYVQPLELKP CGHVTCYACC EQLIKNASKT TAGLPSNAAT LPCPVCRTVV TSIDPPPRIV
ISLLDALEVR CAQCNAVSSR NSYASHECVG TPMNIYDRTI DWGNTLLNKG AWEDAVEEFT
TGIAKFESVT KARDQRKKSG EAAALYSGRA RAQLMLQNID SCHRDADSAV TWDETSAVAH
YLRGAARTKK LGAGETSAIV TAEARIDLER AIALGTLTES DLIDAKGRLA TLLGSTAHRT
EHNNNPSSTS DRLSHTTDGG VRPSTVQDEK KQQPKSGKST SAAATTQQQS KNADATPDTN
TEKTSSHATP VTRERVLKNT LSLLKQAYAL VGDASLDSYD KQNASVREGL LRDVEAYIIA
RPGQTTDEGE DLRVMAYLAP EINITSLCRV EGGLRGLFKQ LVDASLSSLI SSAVNEIMDA
CSSGKNASRS EYLRSHDTDA RKLVVDTITG MEIDLDSLVK TNADMQRIAA EFERKRSERQ
WVPLYIRDLA IHRLSLIADF LLRTIAFAAS SLKIWPSNFP ATRNVHGCLW CGNKGKSTSV
ICDTCQLASY CSVACRQSHS SGHEDVCTVS TTDLEVAMRN VFDTQNATLR NSSVLEKQNN
KALYLKYCSE ESSRADPCGD GDQSPLPPAT TPTCESQQVR GLWAEGLDFD PRRHSNSELF
TAAYVGDPVA VRRVLDKYNK NPSDLKKLVN LRETLMRFSP LHSCIAGARS KPFFGGEFTE
IAKMLITAGS NVHAKDFLGF SCVHHCTTAY ASDESLQILL LLADAGANAN AVNRLDETPI
LEPTNAQKVD TVKTLIMIGA DPNLLACNKR CSAMTLTIML PAMRQVLIRC APLMGLKIGA
TVVFDGLVSK PHLNGKKCVI EQRHVGKFQV RIENTEDSVL CKVDNLRTLS NDSCAKCHKE
LTKLQRCSRC KVTSYCNKEC QESHWAVHKS VCKAVETITI PKVDTADDMN KNGLHVMDLT
QGTSCNPKKR SALVLPSPNV AFLVKIQVPG DLSSGTMTPA FGGNICIYNE SRTLNWSVKE
KHIGAAAYKK LFEFVQNQGV IGLKVYANAQ LTDKGELVVT PVASAVQPW
//
