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Database: UniProt
Entry: A0A286XI96_CAVPO
LinkDB: A0A286XI96_CAVPO
Original site: A0A286XI96_CAVPO 
ID   A0A286XI96_CAVPO        Unreviewed;       887 AA.
AC   A0A286XI96;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Tubulin tyrosine ligase like 7 {ECO:0000313|Ensembl:ENSCPOP00000025167.1};
GN   Name=TTLL7 {ECO:0000313|Ensembl:ENSCPOP00000025167.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000025167.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000025167.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000025167.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; AAKN02004891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02004892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02004893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003478851.1; XM_003478803.3.
DR   AlphaFoldDB; A0A286XI96; -.
DR   Ensembl; ENSCPOT00000048215.1; ENSCPOP00000025167.1; ENSCPOG00000009630.4.
DR   GeneID; 100712966; -.
DR   KEGG; cpoc:100712966; -.
DR   CTD; 79739; -.
DR   VEuPathDB; HostDB:ENSCPOG00000009630; -.
DR   eggNOG; KOG2158; Eukaryota.
DR   GeneTree; ENSGT00940000159078; -.
DR   OrthoDB; 7265at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000009630; Expressed in testis and 10 other cell types or tissues.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IEA:UniProt.
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:SF147; TUBULIN POLYGLUTAMYLASE TTLL7; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   REGION          545..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          413..447
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        545..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  102982 MW;  D3379D8874143CDA CRC64;
     MPSLPQEGVI QAPSPLNLNT ELPYQSTMKR KVRKKKKKGI ITANVAGTKF EIVRLVIDEL
     GFMKTPDEDE TSNLIWCDSA VQQEKIAELQ NYQRINHFPG MGEICRKDFL ARNMTKMIKS
     RPLDYTFVPR TWIFPSEYTQ FQNYVKELKK KRKQKTFIVK PANGAMGHGI SLIRNGDKLP
     SQDHLIVQEY IEKPFLMEGY KFDLRIYILV TSCDPLKIFL YHDGLVRMGT EKYIPPNESN
     LTQLYMHLTN YSVNKHNERF ERDETEDKGS KRSIKWFTEF LQENHHDVAK FWSDISELVV
     KTLIVAEPHV LHAYRMCRPG QPPGSESVCF EVLGFDILLD RKLKPWLLEI NRAPSFGTDQ
     KIDYDVKRGV LLNALKLLNI RTSDKRRNLA KQKAEAQRRL YGQNSIKRLL PGSSDWEQQR
     HQLERRKEEL KERLAQVRKQ ISREEHENRH MGNYRRIYPP EDKTLLEKYE NLLAVAFQTF
     LSGRAASFQR ELNNPLKRMK EEDILDLLEQ CEIDDEKLMG KTAKHRGPKP LCSMPESAEI
     MKRQKYYSSD SSYDSSSSSS ESEENEKEEY QNKQREKQVP YNPKHSSHCK LIQQSNSMRR
     SVSCPRSISS HSPFSGDTRP LSAQQVIPVS RPASASRSHS LNRASSYTRQ LLQNSDASSS
     SSQVSESFRK PKTKEQEDAL TSQTLFVLKD MKIRFPGKSD AESELLIEDI IDNWKYHKTK
     VASYWLIKLD SLKQRKVLDI VKISIRSVLP RIWKVPDVEE INLYRIFNRV FNRLLWSHGQ
     GLWNCFCDSG SSWESMFSKS PEVVTPLQLQ CCQRLVELCK QCLLVVYKYA ADSKGSLSGP
     GPDWGNSRYL LPGSTQFFMR TPTYNMKYNT SGMTRSSVLF TSRYSHL
//
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