ID M2RTK8_CERS8 Unreviewed; 504 AA.
AC M2RTK8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE RecName: Full=Tubulin-tyrosine ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_147092 {ECO:0000313|EMBL:EMD41782.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD41782.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD41782.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD41782.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445791; EMD41782.1; -; Genomic_DNA.
DR AlphaFoldDB; M2RTK8; -.
DR STRING; 914234.M2RTK8; -.
DR HOGENOM; CLU_031301_0_0_1; -.
DR OrthoDB; 100598at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR027746; TTL.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR47551; TUBULIN--TYROSINE LIGASE PBY1-RELATED; 1.
DR PANTHER; PTHR47551:SF1; TUBULIN--TYROSINE LIGASE PBY1-RELATED; 1.
DR Pfam; PF03133; TTL; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT REGION 316..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 56426 MW; 828F26D6A0ABB936 CRC64;
MEEFTALVTW PGAPLTDSLV RKSLASLHPS PKVVTSLSEE LRKSPGNLLQ WANYDSMEHE
LTLAPPPSSK VLSSSYTIRK ALIRKHYLSR CIHNYLTKHP DSPLSDAAPK TWELELSFAD
ELDEMWSDDL WDLGQELDSG SDKWWLLKPG MTDRGMGIRL FRTKDQLASI FESFEQDDSE
EDEEGDDQGN DTSIATSQIR HFVIQEYLSK SLLLDPAEVP LDEQPKPPLQ DLRGHKFHLR
VYCVASGALT IYMYTRMLAL FSGTPYVAPT AGEEGTENVD VNADLAGYLT NTSQQKEHGE
ASVRLFDELI GCHILPPHQP GRPDEASASK SPQPRPSRAM GVALDAEAVR ASRKHETEKR
SQAQEESILT AADVEDIKNQ IAEVLGETFK AALEMSVHFQ PLPNAFEFYG IDLIVSHSEA
PSPRKFQVHL LEVNSEPAIE LTGPRLTWIL EDVFRAMGKV CVEPFFSKSN STDTETAVDA
WEVGQTRHEL RKCLDVQVRG SRGW
//
