ID A0A0N0P2L0_LEPSE Unreviewed; 852 AA.
AC A0A0N0P2L0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPI83076.1};
GN ORFNames=ABL78_7899 {ECO:0000313|EMBL:KPI83076.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI83076.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI83076.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI83076.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI83076.1}.
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DR EMBL; LJSK01000443; KPI83076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P2L0; -.
DR EnsemblProtists; KPI83076; KPI83076; ABL78_7899.
DR VEuPathDB; TriTrypDB:Lsey_0443_0020; -.
DR OMA; SGHSCSW; -.
DR OrthoDB; 156495at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16448; RING-H2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR24007; BRCA1-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR24007:SF7; BRCA1-ASSOCIATED PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 499..540
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 518..630
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT REGION 89..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 92207 MW; 75EB3FD35693DCA0 CRC64;
MELQATMALD RDAVNTVTLR LLPPSTAPTS ATCWLLLHTI PITASLSRTL SRLVSIEEAA
MSQPLPELTS SSATVTAAAV LPTRLADMGT ARGSASRHTT EQPSPSSSPN SSGHTSLDAS
FARMQAAGCV ELVRVGYIVS EIHAYCILLK CHSPPQAVRM KAALEEGAAL GVTAPVEFVS
DARPVTITRR TFAEAGVHEH VPSQADARTD EQRSDGATGD ASHPRAAPTP AAPPPFPQQE
QQQGRPASGD GNDHACAAFD GSSAAGETAP VQRWRTGVHS MPLLDAATMI FPVRDNDDVA
DDEGGFDADD RSHDGRPVPS LRRSAYETTQ QQDSSSASNQ RYRSQLHSPY QPILHRPSGD
QALSPPSSPP FRSQKSPVPA STAATAAGVV TPPMAGAARA RGAMTGLRGA APPPPPHSRL
TAASTASRAS PSPPYAQSNQ HTHTPLHLPM SCGGDACTTP QRLDGSTAKN HRADMSWKGG
HAAEGLLPTA GGCLSGEFCA ICQVDPLRSA ARVTTLCQHS FHLHCYAQLP SGSAECPLCR
FSVYDLLNDA RCEVCGTYED LWVCLICGHI ACGRARRDHQ QQHYRSSGHS CSWQSSTNRI
WNLSSRMFLH QEVALLLDGA EEAQPVPDGH HTSAPAADGD GGELDPLRHM SWAEPFESDL
QEALNESKEE AVARYYTEAL GQLAEEQRRY YEPRLANLRS RRERQRWRAD ALKTEEQVRR
SLEEHEMGSQ NAERQQQGAQ APPLYASVYG VVREERRQRR RVLAEYAPAM VSILQLAQRA
YTTLYNSLKS TRDDAQQQVL LRSHFNSGLV AQMELVQQRT HEAAKKGERS TQAKRAEEAA
LQRSVEEALS AL
//
