ID G3HFS3_CRIGR Unreviewed; 1247 AA.
AC G3HFS3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN ORFNames=I79_009438 {ECO:0000313|EMBL:EGW02806.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW02806.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000256|ARBA:ARBA00036640};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; JH000334; EGW02806.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HFS3; -.
DR STRING; 10029.G3HFS3; -.
DR PaxDb; 10029-XP_007626766-1; -.
DR eggNOG; KOG2156; Eukaryota.
DR eggNOG; KOG2157; Eukaryota.
DR InParanoid; G3HFS3; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0030991; C:intraciliary transport particle A; IEA:InterPro.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IEA:UniProt.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR029302; IFT43.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 1.
DR Pfam; PF15305; IFT43; 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 Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 141834 MW; 4CB4798FB55387FD CRC64;
MPVVMARDLE ETASSSEDED LVNQEDHPCI MWTGGCRRIP VLVFHAEAIL TKDNNIRVIG
ERYHLSYKIV RTDSRLVRSI LTAHGFHEVH PSSTDYNLMW TGSHLKPFLL RTLSEAQKVN
HFPRSYELTR KDRLYKNIIR MQHTHGFKAF HILPQTFLLP AEYAEFCNSY SKDRGPWIVK
PVASSRGRGV YLINNPNQIS LEENILVSRY INNPLLIDDF KFDVRLYVLV TSYDPLVIYL
YEEGLARFAT VRYDQGSKNI RNQFMHLTNY SVNKKSGDYV SCDDPEVEDY GNKWSMSAML
RYLKQEGKDT TALMAHVEDL IIKTIISAEL AIATACKTFV PHRSSCFELY GFDVLIDNTL
KPWLLEVNLS PSLACDAPLD LKIKASMISD MFTVVGFVCQ DPAQRISNRS IYPTFESSRR
NPFQKPQRSR PLSASDAEMK NLVASAREKV PGKLGGSVLG LSMEEIKVLR RVKEENDRRG
GFIRIFPTSE TWEIYGSYLE HKTSMNYMLA TRLFQDRGNP RRSLLTGRAR VNSEGVPELK
VESMNSKAKL HAALYERKLL SLEVRKRRRR NGRLRAMRPK YQVIAQPAEM NIKTETESEE
EEEVGLDNED EEQEASQEES AGSLGENQAK YTPSLTVIIE NSPRESTMKV AEWTNKGDQC
CKIETQEPES KFNLMQILQD NGNLSKVQAR LAFSAYLQHV QVRLTKDSGG QTLSPSWAAK
EDEQMELVVR FLKRASSNLQ HSLRMVLPSR RLALLERRRI LAHQLSDFIV VYNKETEQMA
EKKSKKKLEE EEEDGVNAES FQEFIRQASE AELEEVLTFY TQKNKSASVF LGTHSKSSKN
SSSYSDSGAK GDHPETIQEV KIKQPKQQQA TEIHSDKLSP GAYHPHKHHS GIAKTQKESE
DGSFNRRYNQ SLVTAELQRL AEKQAARQYS PASHINLLTQ QVANLNLASS VINRSSASTP
PTLRPVISPS GPTWSIQPDL HTPENHSSPP GSRSLQTGGF AWEGEVENNA YSKATGVVPQ
HKYHPTAGSY QLHFALQQLE QQKLQSRQLL DQSRARHQGA KMGRRAQQDS TQAESYLSNK
NSSLTQTGEA PPPKPPRRQG GWADDSVKMS KLGKKFSEEM EDRRLRQHSL TGSDEGEDIP
VIPDLEDVQE EDFVLQVASP PSIQVNRVMT YRDLDNDLMK YSAFQTLDGE IDLKLLTKVL
APEHEVREDD VGWDWDHLYT EVSSELLTEW DLLRAEKEDP VGPSRYT
//
