ID A0A3Q7UAD9_VULVU Unreviewed; 1263 AA.
AC A0A3Q7UAD9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN Name=TTLL5 {ECO:0000313|RefSeq:XP_025864430.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025864430.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025864430.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025864430.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025864430.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_025864430.1; XM_026008645.1.
DR AlphaFoldDB; A0A3Q7UAD9; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 1.
DR Pfam; PF03133; TTL; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT DOMAIN 150..360
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 141337 MW; C80B4BE6B3C4C760 CRC64;
MPVVMARDLE ETASSSEDEE VVSQEDHPCI MWTGGCRRIP VLVFHAEAIL TKDNNIRVIG
ERYHLSYKIV RTDSRLVRSI LTAHGFHEVH PSSTDYNLMW TGSHLKPFLL RTLSEAQKVN
HFPRSYELTR KDRLYKNIIR MQHTHGFKAF HILPQTFLLP AEYAEFCNSY SKDRGPWIVK
PVASSRGRGV YLINNPNQIS LEENILVSRY INNPLLIDDF KFDVRLYVLV TSYDPLVIYL
YEEGLARFAT VRYDQGAKNI RNQFMHLTNY SVNKKSGDYV SCDDPEVEDY GNKWSMSAML
RYLKQEGRDT TELYGFDVLI DSTLKPWLLE VNLSPSLACD APLDLKIKAS MISDMFTVVG
FVCQDPVQRA STRPIYPTFE SSRRNPFQKP QRSRPLSASD AEMKNLVGSA REKVPGKLGG
SVLGLSMEEI KVLRRVKEEN DRRGGFIRIF PTSETWEIYG SYLEHKTSMN YMLATRLFQD
RGNPRRSLLT GRTRLAADGA PELKVESMNS KAKLHAALYE RKLLSLEVRK RRRRSGRLRA
MRPKYPVITQ PAEMNVKTET ESEEEEEVAL DNEDEEQEAS QEESAGSLGE NQAKYTPSLT
VMVENSPKEN AMKVSEWNNK GESCCKIDTQ EPEPKFNLMQ ILQDNGNLSK VQARIAFSAY
LQHVQIRLMK DSGGQTFSAS WAAKEDEQME LVVRFLKRAS SNLQHSLRMV LPSRRLALLE
RRRILAHQLG DFILVYNKET EQMAEKKLKK KLEEEEEDGV NTENFQEFIR QASEAELEEV
LTFYTQKNKS ASVFLGTHSK SSKNSNNYSD SGAKGDHPAT MEEVKIKQPK QQQATEIHSD
KLSRFTTSAE KEAKLVYTNS SSASFSGPAA TLLQKIPNTH LSSIITTSDL SPGPGHHCSL
SQISPAVPSM SHQPTVLLST VPDTASPSIH PGTQNVPSPA GLPRCRSGSY TIGPFSSFQS
AAHIYSQKLS RPSSAKAAGS CHPNKLHSGM AKPQREEDGS LYSRRYNPSM VTAELQRLAE
KQAARQYSPS THISLLTQQV TNLNLASGII NRSSASTPPT LRPVISPSGP TWSVQSDPQA
PESHFTPPGN RSLQTGGFAW EGEVENNAYN KATGVVPQHK YHPTAGSYQL HFALQQLEQQ
KLQSRQLLDQ SRARHQAIFG SQTLSNSNLW TINNGAAGRI SSATASGQKP TTLPQKVVPP
PSSSSSLVPK PPANHKQILR KMTSQRVSKG SSADGQLNGL QSSLNSAAFM PITSSTDPAH
TKR
//
