ID A0A3N0XIT3_ANAGA Unreviewed; 691 AA.
AC A0A3N0XIT3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 10-JUN-2026, entry version 21.
DE SubName: Full=Tubulin polyglutamylase TTLL11 {ECO:0000313|EMBL:ROI16651.1};
GN ORFNames=DPX16_22628 {ECO:0000313|EMBL:ROI16651.1};
OS Anabarilius grahami (Kanglang fish) (Barilius grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Xenocypridinae incertae sedis; Anabarilius.
OX NCBI_TaxID=495550 {ECO:0000313|EMBL:ROI16651.1, ECO:0000313|Proteomes:UP000281406};
RN [1] {ECO:0000313|EMBL:ROI16651.1, ECO:0000313|Proteomes:UP000281406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-KIZ {ECO:0000313|EMBL:ROI16651.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:ROI16651.1};
RA Jiang W.;
RT "Genome assembly for a Yunnan-Guizhou Plateau 3E fish, Anabarilius grahami
RT (Regan), and its evolutionary and genetic applications.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:ROI16651.1}.
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DR EMBL; RJVU01074626; ROI16651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0XIT3; -.
DR OrthoDB; 202825at2759; -.
DR Proteomes; UP000281406; Unassembled WGS sequence.
DR GO; GO:0036064; C:ciliary basal body; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IEA:TreeGrafter.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IEA:TreeGrafter.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:TreeGrafter.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF154; TUBULIN POLYGLUTAMYLASE TTLL11; 1.
DR Pfam; PF27858; EF_TTLL11; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000281406}.
FT REGION 72..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 78153 MW; A122390637CB1E60 CRC64;
MLVDYPDIFT NLNEITNHPT IINTMSDHYE RVKIELQQMK AVESEAAADE EQLSPASVTS
VPAEVSFAAR RDLSRSSING RSRSKSRSKA DGHERQVNGK QLSDLTPQKS DYSQEKGQSR
LSNEQNIKGT LRLLKGKTAA NGHVESCQRE KDLKCEHHGK EDGSKVAKKR RAVTVDTSKA
KTSLEALKMS IRQLKWKEFP MGRRTACDIY WHGVSFHDNE NIVSGQVNKF PAGMIEMLRK
INLSRAVRTM QELFPEEYNF YPRSWILPEE YQLFSTQIRL LKDNDSTLKS TFIVKPDSGS
QGDGIYLIRD PADLRVISGS QIKQAVVQEY IQKPLLIDKL KFDIRLYVLV RSLEPLELYI
AKEGLSRFCT EPYQEPSQKN LSHVFMHLTN YSLNVHSGNF VHSDSCSTGS KRTFSSVLYR
IASKGVDIKK VWSDIIALVI KTVIALVPEL KVHYQADIPP GKPGPTCFQI LGFDILLMKN
LKPVLLEVSP GVYEYVPSPV DEEVKVGVIR DTLRLMDPAQ RKQHVTSNTE GGPPEDAIVV
ETGSDEKESL TDSLPSLCLK QVFPKYTKQF NYLRVVERIA AIFLRFLGVK GTMRLGPTGF
RTFIRQAFIE AFFYLAARRF KAVLLREQVL LLLEVCEGAL EGQSHSEKPR PQRSHPTQSS
APNAFSSPAR TRRHHLRHQP LQLSAKANTE N
//
