ID A0A1I8JPD2_9PLAT Unreviewed; 808 AA.
AC A0A1I8JPD2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=UDENN domain-containing protein {ECO:0000313|WBParaSite:snap_masked-unitig_29719-processed-gene-0.0-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:snap_masked-unitig_29719-processed-gene-0.0-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:snap_masked-unitig_29719-processed-gene-0.0-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC -!- SIMILARITY: Belongs to the DENND6 family.
CC {ECO:0000256|ARBA:ARBA00007159}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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DR AlphaFoldDB; A0A1I8JPD2; -.
DR WBParaSite; snap_masked-unitig_29719-processed-gene-0.0-mRNA-1; snap_masked-unitig_29719-processed-gene-0.0-mRNA-1; snap_masked-unitig_29719-processed-gene-0.0.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR InterPro; IPR024224; DENND6.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR13677:SF0; LD41638P; 1.
DR PANTHER; PTHR13677; UNCHARACTERIZED; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS50211; DENN; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..278
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 488..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 89219 MW; ECB72C55BFFF8A2C CRC64;
PDPRSQRSRT TASAAASEEV TLVTSPAPDR VLPTVHEVNL FNALAPLLWE LVLLNAPLIV
MGAGSDTCSN LVQALVNCIF PLRYATDYRP YFTIHDCEFK EFTAKSQSPP SVMLGVTNPF
FAKALQHWPH IVKIGAAMPT DKELKVKRKS SSLKSLDFKP GIYSKYTPYL GVQRGRQIEA
QSVIIRRQFA ELTHSFMIPL HGPRDWPGLY QRFLASPNFA QWLSQRQSEA HAQLEALHAE
ALCGVDLLRW SQGRAELRRT LRRGHRGQIP LSVERLDQLQ FQLDAVIASM PDDLRAVMLS
APQQQQQQLK IMRRCPERCI RIFALLVVGA GGIGCELLKN LVVSGFRRIS IIDLDTSMSM
VAKQSVLKYG RDADITAYHD SVLEEKYGVD FFSGFDIVLI ALDNRAARNH VNRLCLAANV
PLVESGFRRL PGTGEALGVT ACYECKEQQK QKSYPACTNS QHPIRADTLR GVGQVPCLAS
CLVKPIPTRM SRRTPRDPEL SSSSSTTPAV ANGSQANEQQ SQKQTTRSWA EATGYDPSRL
LKKLFADDIR YLLTIAPGGR APYDAVDRRT QLDGSGDGRR RSRRLPAGPR GLVGRRSSAA
TCSARLWISS GVATRKRSSA DDYLVFDKDD QAAMDFVASA ANLRAYAFGI TANSRFTVKA
MAGNIIPAIA TNQRHHCGGS LSVFLEKKLH PRGRIIIPDP APTPSSDCPT VSIFKLSATC
SRSKPPRSRP PPQRRGRLLP VGSGARGSCG IRAARIWRGE ESRLLDEADD DDELEIVAAH
QNRLTGASSQ EPDIFYTIRI ICRASTKF
//
