ID U3JV77_FICAL Unreviewed; 1303 AA.
AC U3JV77;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN Name=TTLL5 {ECO:0000313|Ensembl:ENSFALP00000006681.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006681.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000006681.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000006681.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
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DR STRING; 59894.ENSFALP00000006681; -.
DR Ensembl; ENSFALT00000006710.2; ENSFALP00000006681.2; ENSFALG00000006387.2.
DR eggNOG; KOG2156; Eukaryota.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000162910; -.
DR Proteomes; UP000016665; Chromosome 5.
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; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 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:UP000016665}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 145763 MW; 6AA643C080B0B84D CRC64;
MPSGMAKDLE ETGSSSEEEE DAIDGLEDHP CIKWTGGGCR RVPVLVFHAE AILTKDSYLR
LIGERFHMSY KIVRTDSRLV RNILTAHGFH EVHPNSSDYN LMWTGSHLKP CLLRTLTDVQ
KVNHFPRSYE LTRKDRLYKN VCRMQLAHGF KTFHILPQTF ILPTEYQDFC NTYSKDRGPW
IVKPVASSRG RGVYLVNNPN QIVVEDNILV SRYISNPLLI DDFKFDVRLY VLVTSYDPLV
VYLYEEGLAR FATVRYDQAS KNIKNQFMHL TNYSVNKKSG DYVSCDDPEV EDYGNKWSMS
AMLRYLKQEG RDTAALMASV EDLIIKTLVS AELSIASACK SFLSHRGSCF ELYGFDVLID
DTLKPWLLEV NLSPSLACDA PLDLKIKASM LSDMFTLVGF VCRDPGQRSS RAIYHSSESV
RRNPYQKLQR TRPLSASDAE VKSSVPLGRE KATGRHSSSV LGLTMEEIKV LRRVKEEYER
RGGFIRIFPT PLTWDLYGSF LEHKTTMNYM LATRLFKDRG KMKREFITGR SRAGVNGRPD
MTMEAVDSHA LFYERKLVSL ELRNRRRYHG KARAAQTRAS DTSEPTKLSL KSDMEGEEEV
EVDEDENEEV DRSVCSLSDT QVKNKPKLSE SVKTPSKETL PKKCDKKTED GEELFLQKSD
SESRFNLLQI LQKQGNLSKV QARTAFSAYL QHVQFRLMKE AGEQIQNPAW AAKENEQMEL
IIRFLKRAAS NLRQSLRLLL PSRHLGLTDR RRVLARQLGE FILCYKKETE QMIQKQSKKK
QEEEEGVNPK DFEDFIARAS ESDLEEVLTF YTHKNKSASV FLGTKSPNTK YRNSSHQSEK
QPQGEHPEML KKIKGDHPKS SVADLSAEGA LKGCKPKEAK PSFPEGFTFS LNAEVKLPQC
SPLGASSSVP GATFQRSTSS SGMPPQPAAS ENSKVAGHLS LPAPPAGPRL IQSSPPLPSL
QSTASDSSSV LTSPMSTETC SLAGLHRRSV TYTVSPFSSF QRAAQIYSQR LSSAKVGLHR
SSSGQCVGSA RMHKDAEHAS SQGKRHSPAV LTAELQQLAE KQAACQYSPP SHVSLLTQQL
TSLDLASGAI SKGNAAAPQS HWSPLIKRGS LLPVQSDIHR DDKRPLSSVV RAPENHHFAV
EGEMENSLYK VTRGPLAHPS YQLQFAVQQL QQQKLQSRQL LEQNQARQQA VFANYSQSST
SHISLPAGSD AHKTSSATSS IQKAASLHKV MPSQSTAPQL VPKPPRNHRQ AVIRKAAAQR
ISKVTSTEKQ LNGFQSLHSS ASCEPETYST ASAHREGLTQ NAR
//
