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Database: UniProt
Entry: A0A168JT40_CORDF
LinkDB: A0A168JT40_CORDF
Original site: A0A168JT40_CORDF 
ID   A0A168JT40_CORDF        Unreviewed;      1777 AA.
AC   A0A168JT40;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   31-JUL-2019, entry version 21.
DE   SubName: Full=Chitin synthase 6 {ECO:0000313|EMBL:OAA80843.1};
GN   ORFNames=LEL_00388 {ECO:0000313|EMBL:OAA80843.1};
OS   Cordyceps confragosa RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA80843.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA80843.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA80843.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA80843.1}.
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DR   EMBL; AZHF01000001; OAA80843.1; -; Genomic_DNA.
DR   EnsemblFungi; OAA80843; OAA80843; LEL_00388.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   Gene3D; 3.10.120.10; -; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076881};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    739    756       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    776    799       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1047   1066       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1438   1465       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1471   1492       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1499   1522       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       95    604       Myosin motor. {ECO:0000259|SMART:
FT                                SM00242}.
FT   REGION        1     24       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      338    359       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    338    354       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1777 AA;  197813 MW;  255350F0DBCFBED8 CRC64;
     MANRMSMFSV ASEGPGNNRG PQTAQVSTTT LLNTIHNIYL ASQPHQLDSS TSLVVNTWLT
     ASQGGPTVDA ALATRAWEHA RRRAEDGLIV LGSLHSSAPS VLVPFISSLP FTIPNTIFKA
     FDSVQPFLRC VTPYNPSFPR QAALSATFTL NLAGNLSAAS LALSQGGIDT ENGLFNIPAS
     AGYRAFDVFY YLLTSASTPA EREFLGLQAP STYALLARSS TYTPPTYLPT ADDSASADDF
     RQALKDIGIK GSAHRNFIST LAGLLKLGNT LDYELESESL DELCDEASGL LGLEPEVLTA
     KCSTEDRRIL VSGLYESLVD WVISKANTAI ASQMTRIRDG EESADGRGVR TPTSEEDNGD
     TVNLTVVEIP DPVLGKAVCM RSIFDDSCGI NSEMIQDGVE ASPAGSSVMR EVQQAVADVA
     PDLGIMTGPQ GRDRQRELEQ REVVLERVAH AAEDGGFIKK LLFPVQGEGI NLGRAGRVDL
     PHLLASSRAW YHLSLHPTDD SPSSLAALPS ITSAWSAGTV SRQLRSWRLP EWANRRNRHL
     DYTADFDVEE FVTRYGPLGC TDGRDGIESW MLERGWSNGE IFVGKERVWI RESAWWDAES
     MLDMKQGTNV QGLNNNPFSS GFDTSYSNTG SGFFPPQPID NTYGASRDEL VGGHSRNVSQ
     ANLSQAGFPQ AMNVAPSIAP TGMTGMRNVS KGDYGLGNKG DTYKGDEYVD GGDYNGELDP
     ELAKNKHLET KHTTAGRRAW VAIVWALTFW IPSPLLRYIG RMRRPDVRMA WREKLVLVLI
     IFLLNALIVF WIIVFGKLLC PNFNKAWNKS EVASHQGGKT FWVAIHGKVY DISDWWQQQH
     SDVPQVKTTS DVMQPLNGLI MDDYFVPPLN VACGNLGIKE TTRLTANSTP EYETAVHTSG
     YYARYPDSAL HSDNWYYGTF LPKITTYYHG DLVWSTGDVK SDGKENQHMW AMYGDLIYDL
     TDYFNTVELN TGNDVYQFMD KKISDLWKNN PGQNIKQDLD DALATAKASG DQDSYNKMVN
     SWTCIRNSFY VGKTDFRESA RCTANNWIML AFTILICAII LVKFVAAIRF TSKRRPSPQD
     KFVICQVPAY TEGEESLRKA IDSLTALQYD NKRKLIFVVC DGVITGQGND RPTPKIVLDI
     LGVDPKLDPP TLPFKSVGAG SEQLNYGKVY SGLYEFEGNV VPYIVVVKVG KETEQSGAKP
     GNRGKRDSQI LLLSFLNRVH HRSPMNPLEL EMFHQINNII GVDPELYEYL LMVDADTAVE
     EDSLNRLVSA CAHNAKIAGI CGETSLQNDE KSWWTMIQVY EYFISHHLTK AFESLFGSVT
     CLPGCFSMYR LRTVDKGKPL IISDDVIKEY SVCNVDTLHQ KNLLSLGEDR FLTTLMTKYF
     PSMHYKFVQD AQCKTAAPES FGVLISQRRR WINSTIHNLL ELLRLGDMCG FCCFSMRFVV
     FIDLFSTVIL PATCVYLGYL IYLLASKTGP FPVISIAMLA AVYGLQALVF ILKRQWQHIG
     WMIIYIIAFP IFSFVLPIYS FWNQDNFSWG NTRIVIGEKG NKQVIAVEDE VFDPRSIPMQ
     RWDDYAYASN LPGRRGGYQE KEDSPYMDQY EMDEMKSVYS AAPQGTVLSG MPGNNPYMTP
     HSPAPFANRS STMMHQQDPL MQSRRQSSVV DFQGRQSPYQ DFPQARPSMM NVRSQSNLSH
     IGGNRASSAI GYVGGHRPPM ASDASLANVN IDFRQNSGAT SDGSIIESIQ AVLREVDLDT
     ITKKQVRALV EQRLQTELVG ERRTFLDRQI DRELENM
//
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