ID A0A3B3QZR6_9TELE Unreviewed; 1029 AA.
AC A0A3B3QZR6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Ataxin 2-like {ECO:0000313|Ensembl:ENSPKIP00000011409.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000011409.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000011409.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ataxin-2 family.
CC {ECO:0000256|ARBA:ARBA00007503}.
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DR AlphaFoldDB; A0A3B3QZR6; -.
DR Ensembl; ENSPKIT00000023351.1; ENSPKIP00000011409.1; ENSPKIG00000018462.1.
DR GeneTree; ENSGT00940000157795; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; ATAXIN 2-RELATED; 1.
DR PANTHER; PTHR12854:SF8; ATAXIN-2-LIKE PROTEIN; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 3: Inferred from homology;
FT DOMAIN 164..233
FT /note="LsmAD"
FT /evidence="ECO:0000259|SMART:SM01272"
FT REGION 215..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..707
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 108497 MW; 553A615A733EC105 CRC64;
MLSALIKNLF WENQPKGYCG SQHLPVPSCG STCDIRVKNG SVYEGIFKTL SSRCELAVDA
VHRRCEVAGG SSAPPRREEI TDTMIFSPSD MVTMTCRDVD LSFATRDSFT DTAISASRVN
GEHKEKVLQR WEGGDSNGEN YDLETDASNG WDANEMFRFN EENYGIKSTY DSSLSLYTVP
LERGNSEGFR QREARAARLA SEIESSPQYR HRVALENEDG KTDEDRFSAV VRERDGGERE
RGRESPRERD RGRDSPSCGN REGKYIPLPQ RAREIGTSSS GIRGERGERG ERGGGGATTP
SLPNRMGGYH SSRPAPSSSS PRPPLPASSG QSASSSERSS PLSSRGGYSP HHPQGSPGSG
TAFTSPASLG SGGGFGLPCP GDSPAAPAAP VAASPNSPPA PHGQSGTPSL SHPHTLSDTT
RPVNGVSSRT SPKSQRPVQT SRPLRTAATH STPAVSRPPK SGGSSQDASL AASQYQDTVP
VSMTTKKPPG PAPLFPVDVN EILGSAGKDR AVENLVSLQD VKTPKVTSVQ QRSQIEELRK
FGKEFRLQPS GSSTSTSVAA SAESPQSSPA QTSPAEPVPA PGPKLNVTQD VPQPPAPSSP
SEERAKDKEP EGTVGASAVP TIPAVAPDRQ SPGAPQSART PGSEEAKLET TERVEGVTDQ
VKKSTLNPNA KEFNPNKPPL TLPSKPTSAP TPPRPTPPSP SVVLQPPPGQ GPIYNSTYVS
YMPQIHPPTP LYPYTMSAVN PGKYSRTKGS VVAPRSDHSS SAPPMLQAAA SAAGPPLVAS
PYPQSYLQYS PQQYSQQVIQ SVSPYPGQPM YPVLPAGARM LGTGGGHPQT LGPPGGPQFP
GQGEGPPGPQ QGIYAPQTFS HHSGSMHPPQ PSSTPTGSQP PPQHTAPSPG QSAQSGPQTQ
SLYHSGPLSA TTPPNMPPGH TSPQGSYPLQ GYSLHGHQHI PHTYPPIGQL AQAHVPGALP
GPHHTGTHAH HPMMLLHAPP PQQGPTSGPQ HGPPPQQSTH QHYAYTISHP QVQVQAHPPQ
QLPFHPPGN
//