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Database: UniProt
Entry: D8TIL0_VOLCA
LinkDB: D8TIL0_VOLCA
Original site: D8TIL0_VOLCA 
ID   D8TIL0_VOLCA            Unreviewed;      2481 AA.
AC   D8TIL0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=tRNA-uridine aminocarboxypropyltransferase 1 {ECO:0000256|ARBA:ARBA00039242};
DE            EC=2.5.1.25 {ECO:0000256|ARBA:ARBA00012386};
DE   AltName: Full=DTW domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042508};
GN   ORFNames=VOLCADRAFT_120236 {ECO:0000313|EMBL:EFJ53263.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ53263.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
CC   -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC       (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs
CC       (acp3U(20)). {ECO:0000256|ARBA:ARBA00037050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-
CC         amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-
CC         thioadenosine; Xref=Rhea:RHEA:62432, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:16092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00024168};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TDD superfamily. DTWD1 family.
CC       {ECO:0000256|ARBA:ARBA00038290}.
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DR   EMBL; GL378323; EFJ53263.1; -; Genomic_DNA.
DR   RefSeq; XP_002946268.1; XM_002946222.1.
DR   STRING; 3068.D8TIL0; -.
DR   GeneID; 9621394; -.
DR   KEGG; vcn:VOLCADRAFT_120236; -.
DR   eggNOG; KOG3795; Eukaryota.
DR   InParanoid; D8TIL0; -.
DR   OrthoDB; 315417at2759; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.730.10; AP2/ERF domain; 1.
DR   InterPro; IPR001471; AP2/ERF_dom.
DR   InterPro; IPR036955; AP2/ERF_dom_sf.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR005636; DTW.
DR   PANTHER; PTHR15627; NATURAL KILLER CELL-SPECIFIC ANTIGEN KLIP1; 1.
DR   PANTHER; PTHR15627:SF8; TRNA-URIDINE AMINOCARBOXYPROPYLTRANSFERASE 1; 1.
DR   Pfam; PF00847; AP2; 1.
DR   Pfam; PF03942; DTW; 1.
DR   SMART; SM00380; AP2; 1.
DR   SMART; SM01144; DTW; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   PROSITE; PS51032; AP2_ERF; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          2038..2095
FT                   /note="AP2/ERF"
FT                   /evidence="ECO:0000259|PROSITE:PS51032"
FT   REGION          247..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          937..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1132..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1307..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1416..1437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1450..1476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1705..1729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1809..2024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2190..2288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2332..2353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2418..2481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..748
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1335..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1532..1548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1852..1871
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2481 AA;  247552 MW;  98DEDE5E82DBB543 CRC64;
     MAGLHSVPKL SARRPDWELP ELHGDLQLAP LDPLHNNTDR IKCPKCGRSR AHYCYDCLQP
     LVPFPIVELP FRVSIVTHHE EKPSKNTGVQ VALLAPGQVD LHSMSQVPDD VDPSRCVVLF
     PSDTALEVEQ LEPDSIDRLF IIDSRWKKAG ALMRTETFRS MCAVRLSHTR SAFWRFHTRG
     VSDEGVCTVE ALYFFLEALV KHGKLSDPRF TAPHTFDNLL WYFVYQHQVV QQAALKRLQE
     RGTAELLGQQ PQQQEGPGRA DTEQGQDQPH QQKPQQQQQR KGQTKQQQQQ QQKQKQNPMR
     QTQKQNEQQQ QKKTQKQQQQ GQGQGQGDGP LTNLGGVGGP EVSGISEYGG ANTLAARKGP
     AGNGGDGTTG GKQQQQQVLP SGDQPEESRR QLHAAEDAAV AVVAGPAGRE GKGEAGGGVV
     REDEEIRCGP SGIGPAAAGV WEAGAPGAVH GDGSRNDGGD VDDAEGSGST TLQSGWADSR
     VLPHPFASSN SSSLQVSLEL PPGQFTSPGT LPLHSPATSA PMTATSAVPQ PQPQPETLAA
     VPGVRGVSCV IVDGQPSLGL SPPAAGGGRG ASASGAALPL LPQPPLGSGG VLQLAAPAAG
     AAAATGPTAA ATATVQGSSA PAELTAPTCA SLPALCLPAV ASDVCGLAPV PSGASGGGGS
     GGRVGIDSHH ATGQPAAAGG GAAVVAAGVA MPPQQQHPNP APPQHSGGLS LRRIKPVAAA
     IDLHCALAAR KEQHPVPPPP PHPQPQQQPL LQSPSSAICD ASTSGRPGPY VPQCGLAGGS
     SVLPIAPAVE GVPSAAAAGP AHSGSADGAP AASARAAVAV GLSAGVDGMK GMNAAHSTMQ
     QLPPQQADGG SNETAGEGQV LWAPTAAVNT TADTAPWAGV VSSGHMGPYP GGRADAVGAS
     GSGGGGTATT FTIGCNLLQQ GTGTTTALPC TYGSQARASG GGGGPDAGGG GGGGLVPTDC
     VGPPAGAPIL SGRASDPGVS SFPQQQQQQQ VVLLPPGESA SASPAVKSSA HKAIAAIPVS
     LQQQQQQQQL AGGSTSGGAI ADRFLASLVL PGVGGLTPPT EPASGGFSLP AEAAQEPPHP
     QLQPQHLPQP VAAAAAAPQP QPLLFPPSLG IPPFSPAALQ LMAFSQMGQA VAATAEHQQH
     HQALQSDQQQ QQQQQLAQLQ QHHQAAAALS LMQHMWQAPF GLVMPPGMMG MGMVPGMIWP
     PGQMGLTPAA MPTPGGPLNP AAAAAAAAAA AAQFPALFNP AMMLPALAPF ALPLQAAATA
     AAAQQLQQQQ QQQQQQPAAT VAAVNAAISG RSTAGNAGMT AAAAAVPPAL VKGSSRPTKS
     AVKTEAAASV RGASATQEPA VQKQQQPQQP GGTTSCVGPE AAVRAPPTRC LTPLVPSALP
     SAAAATTAAA AAAHPLVVQQ VRPDFTAFAG APAFSAAEAD SRPGPPPQTE ADDGGGVLAA
     PAAANCRRGN TAAGAATRDG ASGDGNKDNS AVGAADADAE AEVEVAKKAP RSLPGLEVTR
     LQSFASADLV VVDALQLLAA SPPPSPHRER RASGTSGASV TTAGGGGGSR RSSDGGGAAG
     AAAGIGPTAT ADADTTTSGR PHTVPARRMF ELPDPVPVKR EPPQPQSGAA GLTSAAGQGP
     RAAVTSAGEV RGPAATIPAS ARLPWLATSP ALPLPPRAAA AAAGTLDRQR LLHLAAVGAE
     KVRRRASGQG GSGASLVGLE AAATGVADGR EDEPQLALPP GARRPKTRLA RAAAAPGGAF
     LAVILEATEA AAAASAADAE IGGDGEEMET HAGAVATAQG LGLGHSRAPV VAGSQPLSAA
     AVAAIGAGRS ARRSTGSGGG GGTRKVQWAT SEEAPFGSMR SAATAGAEED EGMVQGGEEE
     DVGEEDGEEL EEVAAARGVR QRSRRWRHPA AAAAGSDGGG GGEGDEDDSD EDYNLGREAR
     RRARGARRGG GGAGGATASV FAAARRAARG GGGGGSGGSA VDSDDGEGGL TSDDPAHGYT
     GDGDDDTATA EGAAAAAAAA RRRRSGHGRP PGAGNLRKMK PRRLQSDGRL GFAMRSSRYT
     GVYRTPGGRW RAQFCYRGAV HQLGMYDTER EAAAAWDQAV VTFRGSSSGV QLNLPQLLNS
     YDLQNVREHI HRILDSKIAT TRTKRCLNSY ARNPPGPKSP SRVVPAAVIE NITTEPGTED
     GGDVQLYDGG GDAAASGHVD LSGLPAAAAA AAAGGGGGGV GEVGSSQGRV RTATAAAGRA
     CRRRRSPSPS GDGGPDDSGG DGASGSTAGG CRAARKRAHH DVGGGGGGGG AVLGNSSGGL
     QPHTAAQDNT AGGQQLLLQA QPQRLGALPV GDAALLGLAA LRRHLPLPPP PSVAAGAAAD
     TASLPPPPLR SHDLAGGDVT AAATTDIAAT AAAVATDAAV AAASAAAAVD DVLPPSKRSS
     ETTTTADAAA AAAAAAASLV QPSTHEPWDV EGPAVSKVAA EAQHRSSSSG GGEGGDATGA
     RSGRAASPKR RKSLAIRSRD Y
//
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