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Database: UniProt
Entry: A0A093V196_TALMA
LinkDB: A0A093V196_TALMA
Original site: A0A093V196_TALMA 
ID   A0A093V196_TALMA        Unreviewed;       781 AA.
AC   A0A093V196;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 14.
DE   SubName: Full=Chitin synthase D {ECO:0000313|EMBL:KFX43769.1};
GN   ORFNames=GQ26_0330920 {ECO:0000313|EMBL:KFX43769.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX43769.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX43769.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX43769.1,
RC   ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular
RT   Mechanisms of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFX43769.1}.
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DR   EMBL; JPOX01000033; KFX43769.1; -; Genomic_DNA.
DR   STRING; 37727.XP_002146284.1; -.
DR   EnsemblFungi; KFX43769; KFX43769; GQ26_0330920.
DR   Proteomes; UP000029285; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029285};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029285};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     58     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    103    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    445    465       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    471    490       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    497    515       Helical. {ECO:0000256|SAM:Phobius}.
FT   REGION      663    708       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    663    678       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    685    708       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   781 AA;  88796 MW;  16ABBC887E5E3A88 CRC64;
     MADSADSAPP RPDQWSVADV VYITLVTPLI LAAFAEWFFW LGAFLFGLMN VYRKAEHWTT
     RVIAVFIMIL FSMLRSIFLP VMVVTLPLPN NITRHFSWAL VNLLQWFAFY MFSVLLLVPW
     ALCLYRLITS EIGRSKRIKD VLHDTVAPKV VVVMPVYNEE PGVLIKAIRS VVGSDYPSSC
     LHVFLSFDGE PSDVLWDSIA MQLGIPLGIS KKAQSIDAIY HSVRVTVSRF PHGGKRHCQK
     RTFKLIDHIY ADYVARHDDL FILFIDSDCI LDKPGSGHDM IAMTGIITST TKTMSLITIL
     QDMEYIHGQL FERSVESTCG SVTCLPGALT MLRFSAFRKM AKYYFEDQID KIDDFFDYIK
     CHLGEDRWLT HLFMVSTVKR NQIQLCTGAF CKTQAVQTMS SLIKQRRRWF LGFVSNEVCM
     LTDVRIWRRY PLLCMIRFMQ DTIRTTALLF FIMILSVSTT STSLASLPLG FIAISLGLNY
     ALMLYFGYIL HRFKAWLYPL MFLLNPFFNW LYLVYGCCTA GKRTWGGPRT NAPKADAHTT
     PREAAEQAEA QGDDLNVDVS TFREYGNATV GVPLHPTESV TNRLATDPNY DGTCDVHLDS
     ELSLMEHDRE ECALPKIPLH PRASFDSSTT DNCSVSLPLP VESLVAEERE LYDLYGFDKQ
     TLNGDKEEQR RTPEWKPNLR RDSMSFPGRQ RNSSHQSSPT LSTMPRLDID SSGEVNMEPV
     RQLAPLHLTP SPLGQSCMQN TVPEDDDHEQ TVRAPLFGGI GRRSIKRGRR LFILGRKSES
     Q
//
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