ID A0A0M8ZYT4_9HYME Unreviewed; 667 AA.
AC A0A0M8ZYT4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000256|ARBA:ARBA00030445};
GN ORFNames=WN51_00796 {ECO:0000313|EMBL:KOX72856.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX72856.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX72856.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX72856.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX72856.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000256|ARBA:ARBA00006820}.
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DR EMBL; KQ435812; KOX72856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8ZYT4; -.
DR STRING; 166423.A0A0M8ZYT4; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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:SF39; TUBULIN POLYGLUTAMYLASE TTLL9-RELATED; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 269..524
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 77070 MW; 8C723A6F22EAA17E CRC64;
MELEMEKSTH PSKEKSTNPS SDDISQTHIC KSTYSLHHSS TFVGSESKFC EKAFIKPIRD
NVFEQHVKNY ATNSVHSKIK ERGNSQSNEI PYTYLIVLRT ATRNMSKNTE ARQENEENEE
NEENVSAAGK RNSTTKRRQN GGDKVIRFRC DFPSTQVKVM LARGWIQQCS KCTIKNDDTC
PSRLNLPKPN SKLDEDDLTK RDKVTEPNDP NWHLWWCEVN DVRQALDLKL APHQRIPHFR
NHYELTRKNY LYRNLKRYKK LLLKSNKTDE AELCDGMPLT YELPNDFRLF AEEYHKQPGS
TWIVKPAGRS QGKGIFLFRK LKDLSEWCSK EFGQQVETSP PETFIVQKYV ENPYLLAGRK
FDLRIYTLVT SFHPLKVWLA REGFARLSSE LFDLENIDDS RVHLTNMAIQ LKTQASDDKQ
EPKKGCKWAL TKVREYLTAR HGPDAVEALF QRIAGVIMAS LLAVQPVIMP GKNSFELYGY
DTLLDEDLTP WLLEVNASPA LTGTDTEDYR LKFDLVDDAL NVLDLEARFS GRETRIGGLD
LLWNDGPVWT HCPNPSVCGQ PPTDLRKLNV FLGAWNDRIQ QLRRLGECLE KKKSRVQNDR
AKILWQKTID AHENPLHKRD IAFEKFVIET SSELYSSNYF LMNTRALFFT GFHAIKILQQ
SYESAAK
//
