ID A0A1I8G801_9PLAT Unreviewed; 959 AA.
AC A0A1I8G801;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000313|WBParaSite:maker-uti_cns_0001035-snap-gene-1.2-mRNA-1};
GN ORFNames=BOX15_Mlig013225g3 {ECO:0000313|EMBL:PAA73989.1};
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:maker-uti_cns_0001035-snap-gene-1.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0001035-snap-gene-1.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:PAA73989.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA73989.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA73989.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000256|ARBA:ARBA00004120}.
CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC {ECO:0000256|ARBA:ARBA00006118}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIVC01000983; PAA73989.1; -; Genomic_DNA.
DR STRING; 282301.A0A1I8G801; -.
DR WBParaSite; maker-uti_cns_0001035-snap-gene-1.2-mRNA-1; maker-uti_cns_0001035-snap-gene-1.2-mRNA-1; maker-uti_cns_0001035-snap-gene-1.2.
DR Proteomes; UP000095280; Unplaced.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902}.
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 110181 MW; 72D2FE1E4BE247BE CRC64;
MPKAVVQRQF RLQPVEQQQH QLPEPRPRST RLSSTSATAT TSIPESSNPM PKPRLRQEQQ
QLQQPEPRQR RKRAGAAIVA DEFPKPSSTS GGRQQLARVA FEVGSKGWSV GNSNRLDYSA
NNPDDDEEEA DFDETKLSPF YDGYNTRKLL EKWRDLPPRL TMSDWAFYVK TTRKRSQRSQ
VDKLVADVCS KVLSMRELFH YSLDSGAHCL LWLKSSLAQR FINGMRKGCH IIGRIQGDVM
VKDKQNLSNF MADHQFKEWI ECGPHVCLNE KNEEIKRNLQ RICRHQYTGH YMGKCTDETA
DKECPNFDYY FCECFRRHFF IPEFFTFSHY YLMEEFLKKY ETDVEFQRTT WLAKPAYLTS
SKGFFLIRDA REFRYFYLVR SDTCVRREGF ILQRYLTRPC TINSHKMDCR MYLLLTVTNG
RRVSGFFHPG YVRTTSTPYT VKLEQTKPVS GNIFEHTTAT DLYKLANAKM PGDSDDDDDD
DEKKQCIPFN EACEQITTGA KKVKKGEVEV PMAFANEDEG PGGNLPEKEF EKFHWRFKYI
IEVLCSKMDP MVRDKAGTFQ IFGLDFLIDS DAKPWLLEIN SHVATEQVYD TSQCKVISNV
VTEAICIMCE MFQKSLQEEL IAIEIQQGDQ RLSKLSRSQR MMTAKAEQEA LDKLQVVLDK
TEISKRRPPV FMQNFFWWYD TPRYRWLKPW VLRKKPTPKV LPWHSRVFLG LASRNDAIRR
KNFKADEMTA SHDAMDYFRH IFWREKLEND MRRFEVEKLT KRAEVVASGG ASAPGAGTSV
AGSGGGGGQH SIAGNSGSSK GQQQKQQEQQ QGEQPQSTSN INLASVQPGL RSVMTRRSFT
FDPYQNSDED DEDRHEDGSR IEVDERSALR RVADERGGKS TDDGAFDDAG VDMKPSDLAA
GFFSEDLGKL ANKSNTRRLS LQLPSASEVL NEAEAANNGL GSRSRHRRFR ARFADDTAP
//
