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Database: UniProt
Entry: A0A0L0N8K3_9HYPO
LinkDB: A0A0L0N8K3_9HYPO
Original site: A0A0L0N8K3_9HYPO 
ID   A0A0L0N8K3_9HYPO        Unreviewed;      1789 AA.
AC   A0A0L0N8K3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JUL-2019, entry version 20.
DE   SubName: Full=Chitin synthase 6 {ECO:0000313|EMBL:KND90367.1};
GN   ORFNames=TOPH_05034 {ECO:0000313|EMBL:KND90367.1};
OS   Tolypocladium ophioglossoides CBS 100239.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae;
OC   Tolypocladium.
OX   NCBI_TaxID=1163406 {ECO:0000313|EMBL:KND90367.1, ECO:0000313|Proteomes:UP000036947};
RN   [1] {ECO:0000313|EMBL:KND90367.1, ECO:0000313|Proteomes:UP000036947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100239 {ECO:0000313|EMBL:KND90367.1,
RC   ECO:0000313|Proteomes:UP000036947};
RX   PubMed=26215153; DOI=10.1186/s12864-015-1777-9;
RA   Quandt C.A., Bushley K.E., Spatafora J.W.;
RT   "The genome of the truffle-parasite Tolypocladium ophioglossoides and
RT   the evolution of antifungal peptaibiotics.";
RL   BMC Genomics 16:553-553(2015).
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:KND90367.1}.
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DR   EMBL; LFRF01000013; KND90367.1; -; Genomic_DNA.
DR   EnsemblFungi; KND90367; KND90367; TOPH_05034.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000036947; 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.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000036947};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036947};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    742    759       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    779    802       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1047   1068       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1438   1461       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1473   1492       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1499   1522       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      807    867       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   REGION        1     25       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      339    364       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      651    671       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    350    364       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1789 AA;  198941 MW;  8EFD6372C2706594 CRC64;
     MANRMSMFSM ASESPGGSRA GGPQTAQVST TTLLNAIHNI YLSSQSHQLD ASTSLVVNTW
     LTASQSGPSI DASLATRAWE HARRRAEDGC VILSSLHQST PSVLAPFLSS FPFAVPSSLY
     KALDAIQPFL RCVTPYNPST PRQAALGVTL TLNLTGNLTA ASLALSQGGL DTVNGLLNIP
     SEAGYRAFDV FYFLLTSAST PAEREFLGLR SPSTYTLLAR SGTYDPPSYL PTADDAASAD
     DFRRALKDIG IKGSAHRDFI STLAGLLKLG NTLDYSIESE ALEEICEDVS GLLGIEPDTL
     LNQCSTEDRW TFVGGLYESL VDWVISKANE AXAAQMVRIK AGDESPDGRG VRTPTSNEDS
     GNGDTVSVTV MEVAHTTLGK ALSMRSIFDD SQGINAEMIE DGVQASPAGS SVLREMQQAV
     SEVSPDLGIM AGREGRERQH ELEKRELVLE KIAFASEDGG FLKKLLFPIR GEGINLGRAG
     RFDLPAVLGS NRLWYHLSLH PTDDSPSQLA ALASITSAWS AGTVSRELRS WRLPEWANRR
     NRNLDFTADF DVDEFVQRYS ALGCKDGKDG IESWMLERGW SNGEVFVGKE RVWMRESAWW
     EAESMLDLKP GDNNPAMQGL HSNPFGTGFD TGYSANGSGY FPPQAMDTSF NGSNDQLVHS
     RNFSHGNGSQ LTLNQAPNIA PSIAPTAMRN VSNGDYGLGS KGDTYKGDVY YSEQGEFTGT
     MDPELAKNKQ IETKHVDLGR RVWVGFVWAL TFWIPSPLLR YVGRMRRPDV RMAWREKLVL
     CFLILLMNAI IVFWIVAFGR LLCPNFDKAW NRNEVATHQG GDDYWVSLNG KVYDLSNFWR
     RQHSDTDIQT TSDNMQPLAG LDMDEYFPQP LNLACRGLGI ADTTRLIANT TPEFAIAVHT
     SGKYQPNPTS ALFKDDWYWT TFEPAIKEFY HGDPVYSEDF VSSSGKDSQR MWARYDDKIY
     DLTDYFHTQD VFKNVATYKF LDGSVSDLWK NNPGQDIKRL LDGVIRDSVA NQTEHALVMN
     SWLCIQRVFY KGMTDFRDTP RCTVNNWILL AFTIILCAVI LIKFIAALRF SSKRRPSPQD
     KFVICQVPAY TEGEDSLRKA LDSLTALQYD NKRKLICVIC DGVIVGQGND RPTPKIVLDI
     LGVDPKVDPP ALPFKSVGGG SEQLNYGKVY SGLYEYEGNV VPYIVVVKVG KESEQTKSKP
     GNRGKRDSQI LLMSFLNRVH HRAPMSPLEL EMFHQINNII GVDPELYEYL LMVDADTSVS
     EDSLNRLVSA CAHNAKIAGI CGETSLENDE KSWTTMIQVY EYFISHHLAK AFESLFGSVT
     CLPGCFSMYR LRTVDKGKPL IISDEVIKEY SVCNVDTLHQ KNLLSLGEDR YLTTLMTKHF
     PFMSYKFVPD AQCKTAAPES WGVLVSQRRR WINSTIHNLV ELMRLKEMCG FCCVSMRFVV
     FIDLFGTIIL PATCVYLGYL IYRVVSHTGQ FPLISIVMLS AVYGLQALVF ILKRQWQHIG
     WMIIYIIAFP IYSFVLPIYS FWNQDNFTWG NTRVVIGEKG NKQVVAVDDE GFDPRSIPLQ
     RWDDYAMSNN LPGRRGGAQE KQDYGYGDQY EMDEIKSVYS AAPQGSILAG MGGRSAYMPP
     QSPALGGPAN RASTMHGAYQ DPAMSVRRQS MMSMGTAIHD MGRSQSPYQD MPANRASVMI
     LRSQSNLSPS MGLPAYRSAS ALGYAGGHRS PMGAEAMQST ASFDFQRGHV AAEDTAIVEA
     IQSVLREVDL DTVTKKQVRA LVEQRLQTEL VGERRTFMDR QIDRELENM
//
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