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Database: UniProt
Entry: D8UC89_VOLCA
LinkDB: D8UC89_VOLCA
Original site: D8UC89_VOLCA 
ID   D8UC89_VOLCA            Unreviewed;      1153 AA.
AC   D8UC89;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Acetylglucosaminyltransferase {ECO:0000313|EMBL:EFJ42658.1};
GN   Name=elg26 {ECO:0000313|EMBL:EFJ42658.1};
GN   ORFNames=VOLCADRAFT_97248 {ECO:0000313|EMBL:EFJ42658.1};
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:EFJ42658.1, 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   -!- SIMILARITY: Belongs to the pinin family.
CC       {ECO:0000256|ARBA:ARBA00010386}.
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DR   EMBL; GL378380; EFJ42658.1; -; Genomic_DNA.
DR   RefSeq; XP_002956309.1; XM_002956263.1.
DR   AlphaFoldDB; D8UC89; -.
DR   STRING; 3068.D8UC89; -.
DR   GeneID; 9619130; -.
DR   KEGG; vcn:VOLCADRAFT_97248; -.
DR   eggNOG; KOG1022; Eukaryota.
DR   eggNOG; KOG3756; Eukaryota.
DR   InParanoid; D8UC89; -.
DR   OrthoDB; 313809at2759; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR039853; Pinin.
DR   InterPro; IPR006786; Pinin_SDK_MemA.
DR   PANTHER; PTHR12707:SF0; PININ; 1.
DR   PANTHER; PTHR12707; PINN; 1.
DR   Pfam; PF04696; Pinin_SDK_memA; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:EFJ42658.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        436..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          800..903
FT                   /note="Pinin/SDK/MemA protein"
FT                   /evidence="ECO:0000259|Pfam:PF04696"
FT   REGION          513..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          832..876
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        513..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..999
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1064
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1105..1122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1153 AA;  124337 MW;  88873B434182C887 CRC64;
     MQPSVPLQFR AGFVAYIALS LGIILVLIID PLIDKPVGLI KLRHFTRKQL SHGLNACSWD
     YEGSWRIGFA RGSPDPMHLD VSPEPVITCA NLANATAVSF VADPFLFIPD RSIAPLTAAI
     LLANSTFGNG AKRGDDAGGG GDGLPWFAFY EMKNLARYIG ELGVAVSYDD GATWLHLGTA
     LAESFHLSFP LVLYDSTTEQ YLMFPETSAA RDGAVRVYGT SQETFPFGWQ LLSSRQLDDP
     GWAATRRWFQ FGAPAKYVDT APVWFRSRWW IFTTRVGSPP ARQPKYTLLL YTADELLGEW
     RAHPSNLAGA ASLKANGGRV PYGIDADPRY ARNGGRPFVL GDALYRWSQD CSRYYGEALV
     LLRADVANES SYVERVVTRY EPRRDGVSWN AERVHHADLQ LLPDGTWGGF VDGDRYADGM
     AFFIEREQWF LELKALLLRL AMLQLFLVVV AVAMMYAGYW EAIERIGPSG GGVAVVAAIS
     LPTQKIKQGM AALDPAVLER ELEALRRQRY EASQRVQASR QPLSGTATQA RNASGDAALV
     PSRPALGSGR FGPERGFSGP PPLRGGVADG PRAASTLREG PLSGRLGSGP SPRGLPGGAG
     PHDGPSRGSL RFHGGSGPSS GGGGRGFRDH EDAAAVAVAA PPPRRRAVLS VVVSDHAPQQ
     QQQHEAAHAD KTGQPDSRRE NVPGRGDADR DRDYHHGHHR ARDGDSDRDL SRGRRLGPAL
     VGDDDRDLGR SRDRGWGWDE DRRRREYGNQ DDGHEHGYGG AGGRGTKRPA PAAAADADGA
     GAGSAAAGAA AAAVVVEDPD SRKRARRLLG RTLLGTLQRF RQEDAAFQAS DAAARRAELA
     RKAEEKAAAE AERLRRQAAE ERARKRQEEL DALMDLNLAT DIKVLELLYA KKLARRRALA
     AFLRADGVPA SDGNGNGYGN GNGGAGKTFP QQYQPQAVYW LPVSHCPSTL ALKERQEQEL
     KDWEEAVLAE LELEKDGLRL RSKARRQGIA ERRQRAAEAR TTGRAGAAAA AEGTTVEGRE
     DEDVAEEDRE ALEAVELDAH HEDVEVEEEE VDEQEHEVEV EAAEEPSDGG GGTADAAAAA
     AAAAEEEEEE EAVRAGSGAS AAKAKAEENG KEKERKVSKG RELAMGEVGG GETAKAAVVR
     DDSDSGAGDD EMA
//
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