ID I7MAB1_TETTS Unreviewed; 1554 AA.
AC I7MAB1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Tubulin-tyrosine ligase family protein {ECO:0000313|EMBL:EAS04250.2};
GN ORFNames=TTHERM_00299600 {ECO:0000313|EMBL:EAS04250.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS04250.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
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).
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DR EMBL; GG662449; EAS04250.2; -; Genomic_DNA.
DR RefSeq; XP_001024495.2; XM_001024495.2.
DR STRING; 312017.I7MAB1; -.
DR GeneID; 7837051; -.
DR KEGG; tet:TTHERM_00299600; -.
DR eggNOG; KOG2157; Eukaryota.
DR InParanoid; I7MAB1; -.
DR OrthoDB; 100598at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
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; PTHR46069:SF1; LIGASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR46069; TUBULIN TYROSINE LIGASE; 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 Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:EAS04250.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1524..1553
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1554 AA; 177455 MW; 368C9538B26E3D20 CRC64;
MNNESNVYIR KSKNIKQQAV PRNSDEIDMG NSRRANEKEN SSRLYQNIGG SLMNNIGLDQ
IKIGNTSQYY SAGGTQTNLP SHMGLSQNSG ISNQTTNSQG SNSTQNVILT VTRIVPYQQH
PSQTQQLQQQ ILNHQQQQQL MSSLQNNMLQ SSQFQQQSGN QNIYYQNYQQ SNSQKGQMNS
PTRRFVQNQK PLQNGQSKKT QSIGNIQQQQ QQVTNASIEK TNETDDVNSP GGPRQISIHY
LNGQSSFQGQ VQQNNLSGQS MGVHYNAQKK SMNHIEMEES GGQGADQSGN CSGLDKSPKF
KPQTKFPPIT KGSSAQSSQN TSNYKLQKIK MQDKEVRKNI VALDSISRMD QFTGLNQVGG
VLGNNTFKIL KQGQQQGSYY NQFNKAIQES NGILAVGNSL NQLDMDIKGI IPQENPHYYP
SYKVKRANPN QKHSKDFHTN KDTKENGDNL YLEVVNSKQM NEVNHNFISS QQEFNQNYPS
TAGQGEGREN KFIENYSAGQ EDANSNDINR SSSTPMLLKK EATKRLEKIK HHNTIEGNGN
ENEQQNNRYE KITSQKINAV LGSNSSKHVV TIQKKEKSKL NLNRFEDSDR ESDHPQLNPL
TQKKYSHNGQ SVNAKKPISG AIQANTSLKP IKILKKQQEG ELSENQNAET VSIRSSNIDL
QQTPQQSVKE SGKKAPKEEQ ISSSNNTNQE EDYQGDDEDF KGSSNLSNQA KQNYQNNKGT
DFFKINPKEN QLNQNERASS NIKGAIITND QSSFEKTPQM RKKTYQQKQA MNLGNNQIKQ
NGELDNILND SIQKAPLNIK TTKEKEAKLS EQTIQNNADI NASNKKKQKK KKKRNTLVGP
QGGQNNGLSS LNQGQMKNGQ LVGKYDNLPK EVQRINQYQD FIRAVNFSNN IDVIPIQKPC
FKMYVGKGNN SYLIKSSVKQ RWWLQLETNK DKVDQCHIVW TQLRFNEFLN NLKAFTGPRI
TTDNQILGSE QKINIKTNDS FADTNNNNDA STNFENSPLL DHKMNSSINK DLDSQSQLQG
DLGNAIDSSD SETEKLRSLT SRPTVKKSNS LNNSLSSLKA ELKKGSPNPG TANSQPQNKE
TRSLTPSTRG NAPQNQLKVQ ATYNVNAKRL FHPNDFKKIM EIQPNKDYDL RYFFSQSLPD
QFQQFQKEFD TFQDPNSLKM HNHLENNWNL SNKKALFYNL RNYYTTIKQN PFENIPLTFH
IKDGINDPEY TKFLEHWKQK EDECNQKEKL RLEYKYSSDK AKQSIGSNMK KPRNIWIIKP
GEITNRGTGI TVLNEIDQIT QLLAKNDLHP NGKPKTYIVQ KYLDNPLLYN KRKFDIRCYL
LVTVIKGRMK AYWYQDGYIR TSCKEYNCKS LTNKMIHLTN DAVQKKCEDY GKYEPGNKLS
YNDLQRYLDQ NHTEQKINFQ TVIYPRMRQL ALDCIKSTFL KMDPQRREIT FEVFGLDYMI
DEEFKTWLIE VNTNPCLELS SPLLARIIPA MIENAFRIAI DPIFGFPPIN DWSASAKKTF
IPDSIMENNK FELIFDEAFD GPSLQALFAQ YNEQQQDIII EEEEEEEEEI EDEQ
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