ID A0A3P9NWN1_POERE Unreviewed; 1254 AA.
AC A0A3P9NWN1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000013981.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000013981.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000013981.1};
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 RefSeq; XP_008398484.1; XM_008400262.2.
DR RefSeq; XP_008398485.1; XM_008400263.2.
DR RefSeq; XP_008398486.1; XM_008400264.2.
DR RefSeq; XP_008398488.1; XM_008400266.2.
DR RefSeq; XP_008398489.1; XM_008400267.2.
DR RefSeq; XP_017157984.1; XM_017302495.1.
DR AlphaFoldDB; A0A3P9NWN1; -.
DR STRING; 8081.ENSPREP00000013981; -.
DR Ensembl; ENSPRET00000014126.1; ENSPREP00000013981.1; ENSPREG00000009465.1.
DR GeneID; 103459050; -.
DR KEGG; pret:103459050; -.
DR CTD; 23093; -.
DR GeneTree; ENSGT00940000162910; -.
DR OMA; TRLFQDX; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000009465; Expressed in head and 1 other cell type or tissue.
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; 1.
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; 1.
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:UP000242638}.
FT DOMAIN 139..391
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 141288 MW; 289B7B47E325C0A1 CRC64;
MPAVVREKED SESSSEDEHG EHPCVAWSGI SRTIPVIVFL PEAVVSKNRR ICSVGERYNM
SFKIVRTDSR LVRRILTNHG FHEVHPNSNN FNLMWTGSHL KPYLLHSLQE FQKVNHFPRS
YELTRKDHLY KNIQRMQQTY GFKNFHIIPQ TFVLPSESEE FRSCFAKDKG PWIIKPVASS
RGRGIYLVNN PNQILMDENI LVSRYINNPL LIDEYKFDVR LYVVVTSFNP LLIYVYEEGL
ARFATVKYDQ TTTHIKNNFM HLTNYSLNKK SSDYISCDDP EVEDYGNKWS MSAVLRFLKE
AGKDTTLLMR QVEDLIIKAV LSAELQIATA CKMFVPHKAN CFELYGFDVL IDSNLKPWLL
EVNLSPSLSC DAPLDLKIKA SMIADMLSLV GLVGQDPLLK QPRSDRFTND KKAGPRVQHR
TGVSSETNGD KQKTKSLEES TLNLTTEEIK VLRRIREEYE RRGGFIRIFP TQDTWELYGA
YLESKPSLNS LLAKRLFHGR PMNRNTHLMA DTIRGRHVVQ YERKLLSLEA QKRKERHLTH
HTATRGKKRR KESKAFLAEN RSPETEECSQ EEIEEVKQPL EPLPLKVLVM EQSKQAATPL
EQSHNKPESS SDAAVQNARP AVNLRNVLQQ GRDLSKVQAR VAFSSYLQRV QRRLLVESKT
NSMPNWPDDN NDQMELVIRF LKRAAINLQQ DINIVLPNHQ LPLQDRRRIL SFQLGEFIHC
YNKETELMSK QERGEEEHCV NESVFQEYIT EASENDLEEV LTYYTHRNKS ANVFLGNKVR
SVKTQDSGSR ANSKTLSVTK EDSRASESSL SAGKVCSDPN VKSSETQLLV LRSDQQAEVT
ASKTQPDVRS SQHCSGFSPS SDCANIHPQR CSPTTKSIPL HCPPPPPPPQ PPSYAQSLAK
SNFCHSETLS DPPAYTSAPV ITQPPKVNRT PASTTSNGAS AVPPSQALRK IQSATTPTTN
SKTTFAVPSA IPLYSQTFSR PTSAHQGMYR SRSKPKSNSE GTLRDLQSLS AQAQSNQQAF
ISALQKLADK QVARHYASSS HINLLTHHLT NLNLANKMLG RESHTLTPKA AAIHKPVRTA
QAGKDYLAST RPLQTQSAPN VVMGLNSTQS SQSTKGSYQL QFAIQQLQQQ RLKTHQFLDR
DHPRHQTQFH DQTSSPHPQV STKPSGCPPS SLHVRSSHSQ TSVSPAFAPK PPSSALEGQG
RKTATKRLIK QMSSESSASG SMSSSQQVVY EAICGKTGFP AYSRLFQVQQ PSHR
//
