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Database: UniProt
Entry: K1VY33_TRIAC
LinkDB: K1VY33_TRIAC
Original site: K1VY33_TRIAC 
ID   K1VY33_TRIAC            Unreviewed;      1835 AA.
AC   K1VY33;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   31-JUL-2019, entry version 39.
DE   SubName: Full=Glycosyltransferase family 2 protein {ECO:0000313|EMBL:EKD04437.1};
GN   ORFNames=A1Q2_01213 {ECO:0000313|EMBL:EKD04437.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04437.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD04437.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04437.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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:EKD04437.1}.
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DR   EMBL; AMBO01000224; EKD04437.1; -; Genomic_DNA.
DR   STRING; 82508.K1VY33; -.
DR   EnsemblFungi; EKD04437; EKD04437; A1Q2_01213.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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   Gene3D; 3.90.550.10; -; 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; 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; PF00063; Myosin_head; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01117; Cyt-b5; 2.
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.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006757};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW   Transferase {ECO:0000313|EMBL:EKD04437.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    980   1002       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1247   1268       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1642   1660       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1667   1690       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1696   1720       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    799       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN     1007   1067       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   REGION      684    706       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION      856    879       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1772   1835       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1773   1791       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1792   1815       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1835 AA;  205131 MW;  DB6B3AC8826FB827 CRC64;
     MASGGHGFVP SQAAQYADLT TLISSPSGDG ESSAKVYPNE DTIAALLHAR CRAELPYTRV
     SASGTDYVVV NPRRHLQCLN EESRKGYEED ITTTDGGVGN EPRQPSAYEL AGRVWLLMSR
     RRDGLTASGK STTLRHVTSQ ILSLASVTKA QKRTSDQISH LLTLLESFGN SKTPINPSAS
     QHARYLELHF SLDGELAGAK VLPFGLNKYR IGHLEPEERT FHVFYQMLAG ASPDEREELG
     LDDPDTYALL SSSNCYVLPA GPFSDDSTQL GELRAAFASL GFKAKHVRSI FSVLTAILVM
     SNITFHDEKQ DGSLGMVSYE ERTQVNERGL LYEVAGHLGV NPEELEAVLT NRTKWVSHDL
     ASVFLDAENA ALQRDSLMRD LYAILFAFVV EMANKKLAPG ADTPPGLQIA QIDLPGHQSR
     TQETEVDPRR STLLQQATLI NASGNNGFDE FAYNFNNELL HSYLLRRAFD DQLNWNLDVT
     EDGIRLPPVI PHDNNASVEL LRGGLLGSAR LAKQPAGVIG AIAGVGEQIK GEDREDVKAK
     TVVGTLTTMF TGQPAFNPNP TGGLGMTPRQ GRMFGISHYA GQVSYDATDF IDHNADVFDK
     QLVNLLRNSH DSFVNKLVSG PALATEGHPL DDNIVVEAQV SSTPLRTPTP IVNCITGTAP
     MDHVEWAIDD SIPQPVTAQL NATMATLLDV VDRTRVWGVY CIRPNDSGHA NSYDRKRIRS
     QVRTLQLPEL VNRRQVDYVA EYSLSQFCVR HALPVQDGHA AVEDFARHNG WMPGVDYAIG
     NERIWLAWGA WRQQEDMIRA TETRHGSGEE TLTDEEGGFM SRNASTFGHG RYGDAVDSTE
     NFRRSESMDN LLARSGTQET YGDGHGGGGG GGGRGGNYGY GGLESPNPND SEVWETSKDG
     PYESLNDKDA AAVAAVKRGD FVQSEKRHHA TEIVETSRAR RWWIRITWTL TWWIPSFLLK
     WPGGMKRADI RMAWREKVAI CMMIAFLCGI VIFYIIGFGQ VLCPDMDKAW NKTDLSKHQG
     DDDYYAAIAG KVYDFTKFYK GQHSDMDFKT TSQIMLQFAG QDLTGYFPPP ISVACEGLAN
     KDFTFQKANF TPIMPQAIHT SGVLQTDNDT KLHDENWYWD TLQPKLKKYY KGTYVHDKKD
     LSQGAAEDPT RFWGTYKSKV YDISDYVATN DLYASGSGYE VKYDFLNPDL VSIFQTSSGQ
     DLTKQIDDLM ESWNSDTVNL HFNCLNNAFY LGDVDFRKTA RCTVQNYLLL SFSILLMSTI
     LIKFLAALQL GSKRQPELLD KFVICQVPCY TEGEESLKKT IDSLAVLNYD DKRKLIFIIC
     DGNIIGSGNN RPTPRIVLDL LGVDPKLDPE PLLFKSIGEG SKQLNYGKIY SGLYETEGHV
     VPYVVVVKVG KPTETSRPGN RGKRDSQVLL MQYLNRVHFD APMCPLELEI YHQMRNVIGI
     DPTFYEYIFQ VDADTTVTPD SLNRLISCAA DDQKIIGICG ETKVANERES WTTMIQVYEY
     YISHHLTKAF ESLFGSVTCL PGCFSVYRIR TADKGRPIII SSVVIDEYAE PNVDTLHKKN
     LFSLGEDRYL TTLMMKHFPT FKMKFSPDAI AYTVAPSRWN VLLSQRRRWI NSTIHNLVEL
     LFLPEMCGFC FFSMRFMVFV DLLGTIILPA TFTYLVYLII ICATHKAAVP IISIAMIAAV
     YGLQAIIFIL KREFMLIGWM IVYIIAFPVY SLFLPVYSFW SMDDFSWGNT RRVVGEGKDK
     TIVYDDEERF EESMIPYRTF KEYEANAWEA ASLPSDEERD EKSDAGYSRR TRRTRNTASN
     LAPSIHSSAP SYVGSRQPSP GPYGAQLMPM APMSN
//
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