TTL6A_TETTS
ID TTL6A_TETTS Reviewed; 1195 AA.
AC Q23MT7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable beta-tubulin polyglutamylase;
DE EC=6.-.-.-;
DE AltName: Full=Tubulin-tyrosine ligase family protein 6A;
GN Name=Ttll6a; ORFNames=TTHERM_00284020;
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
CC -!- FUNCTION: Probable tubulin polyglutamylase with a strong preference for
CC beta-tubulin. {ECO:0000269|PubMed:15890843}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15890843}. Cell projection, cilium
CC {ECO:0000269|PubMed:15890843}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:15890843}. Note=Associated with microtubules
CC from cilia, basal bodies and cell body.
CC -!- DOMAIN: The flexible c-MTBD (cationic microtubule binding domain)
CC region mediates binding to microtubules. It is positively charged and
CC becomes ordered when bound to microtubules: it interacts with a
CC negatively charged patch on tubulin. The presence of positive charges
CC in the c-MTBD region is essential for proper binding.
CC {ECO:0000250|UniProtKB:Q6ZT98, ECO:0000250|UniProtKB:Q8N841}.
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DR EMBL; GG662656; EAR98012.2; -; Genomic_DNA.
DR RefSeq; XP_001018257.2; XM_001018257.2.
DR AlphaFoldDB; Q23MT7; -.
DR SMR; Q23MT7; -.
DR PRIDE; Q23MT7; -.
DR EnsemblProtists; EAR98012; EAR98012; TTHERM_00284020.
DR GeneID; 7847221; -.
DR KEGG; tet:TTHERM_00284020; -.
DR eggNOG; KOG2158; Eukaryota.
DR HOGENOM; CLU_272087_0_0_1; -.
DR InParanoid; Q23MT7; -.
DR OrthoDB; 1251554at2759; -.
DR BRENDA; 6.3.2.B24; 6245.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:UniProtKB.
DR GO; GO:0018095; P:protein polyglutamylation; IDA:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Ligase; Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1195
FT /note="Probable beta-tubulin polyglutamylase"
FT /id="PRO_0000249320"
FT DOMAIN 350..703
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..756
FT /note="c-MTBD region"
FT /evidence="ECO:0000250|UniProtKB:Q8N841"
FT REGION 783..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..103
FT /evidence="ECO:0000255"
FT COILED 144..260
FT /evidence="ECO:0000255"
FT COMPBIAS 43..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 500..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ SEQUENCE 1195 AA; 139535 MW; 580D6F2A024B0111 CRC64;
MSQKDIYNKY SNQSADDQQE EDDDENQESS CQLSPEKDLG ESLQGEDLDE DQGVIGEDDE
EQEESYDEED EEEDDEENNQ DQQNNSESNL QYDKTNQKNQ QTEMTDNQNE FLAEDYLSQI
KTNEKSELKY QLDIQSNLSG ENVQDMDEKL KQYIELNGKN ENQQAAESKK IENDEIMKKS
EENVHEKVVD NNQKLNIQQN NINDYQEDIK KDQSNNLVDI QQNNEIIKEV NSEDQQQKNE
MDNKQSDIVL AQEESKQSEQ VEAPIVKQKK IELRPKVIYD PKNDVDQYTG DYSDSGESDE
EANNEDDDED EDDESENESR SRKNKAQLLK KKNNKKEQAK KQQVKKVYKK QTLVLNVADT
KYPVVKFVGK KIFKWKLAYD MESMDFDIFW TDNAVQPEQL GRMQPYQKIN HFPGMFSLAR
KNHLARNLMK MRKQFPDQYK FFPQTWLLPA EYNDFKNQFE KSRSQQKIFI VKPEASCQGR
GIFLTRSLDD LNPSDHYVVQ RYLNKPYLID GLKFDFRLYV LLAGCDPLRI YLYYEGLTRF
ATEKYQEVNR DNIEDMCMHL TNYAINKDNP NFKFNKDKEK MDVGHKRSLT SVLQLLEDQG
HDVNKLWKDI KRVLIKTIIS AQPTLAHHYK SCQPDNFMNN MCFEILGFDI ILDSHLKPWV
LEVNHTPSFS TDTPLDSYIK KNTIRDSLKL MNCTCKAKNE IINQRKEIMQ KRVLTGKKVK
YTPEEKLEEI KKAQQKRDEY EDKHLGGFER IFPMEDDEDD NFTEYMQYAL KCYEEQTGAN
IRRNTKKVTE DPKKITNQPK KLNQPKDLEK IYNTKIGAKL PPRKPNSQTT INKGIPGQNG
QRPSSSQLNE EGETIQCEDQ EQNKDEAIEN AITRSASGRM HDFRIKKQNS PYNIHQKFKN
KIQNRVAIGV KELKLAEEPF QFEENINGKP SNPNVKKIQA YITSEKEQLE IKNMNILQDQ
NYNSSRAVQA KKPQIEPQVL FVQEPQTKKL QILNQAKPPQ QKLQFQLIDN TAAQMEEERR
QWLIQAQRNL QYQLSQQQYQ PQQKLTLLPK GPPIHPQTNV MQSIADIPNS SNSKEILAAV
GGAISGQYKT DKRVTIKQKG QIQNQSINQL KDNNGLFLQP KLFEIQSFQS SQQQQAQQAI
QSSLDQNLIG INQNMVGLND LFVSGKSHKV QPHYQAQQDS YSYQKHNSYS NYYQK
