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Database: UniProt
Entry: K5VYG4_PHACS
LinkDB: K5VYG4_PHACS
Original site: K5VYG4_PHACS 
ID   K5VYG4_PHACS            Unreviewed;      1896 AA.
AC   K5VYG4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   31-JUL-2019, entry version 41.
DE   SubName: Full=Glycosyltransferase family 2 protein {ECO:0000313|EMBL:EKM56628.1};
GN   ORFNames=PHACADRAFT_253847 {ECO:0000313|EMBL:EKM56628.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus)
OS   (Peniophora carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM56628.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM56628.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM56628.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa
RT   and P. chrysosporium, to elucidate the genetic basis of the distinct
RT   wood types they colonize.";
RL   BMC Genomics 13:444-444(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
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DR   EMBL; JH930471; EKM56628.1; -; Genomic_DNA.
DR   RefSeq; XP_007394470.1; XM_007394408.1.
DR   EnsemblFungi; EKM56628; EKM56628; PHACADRAFT_253847.
DR   GeneID; 18915896; -.
DR   KEGG; pco:PHACADRAFT_253847; -.
DR   InParanoid; K5VYG4; -.
DR   KO; K00698; -.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000008370; 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:UniProtKB-UniRule.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 3.40.850.10; -; 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; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036037; MYSc_Myo17.
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   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01194079};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008370};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874053};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01033784};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Transferase {ECO:0000313|EMBL:EKM56628.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    905    924       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    945    964       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1207   1226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1602   1623       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1629   1649       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1661   1680       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        6    756       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   NP_BIND     106    113       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      635    657       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION      760    865       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    760    777       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    804    818       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    826    856       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1896 AA;  213613 MW;  8AC8BC56AEE475C8 CRC64;
     MHQQLEAVTD LATLPSVSDD IVVSCIRERF MADTIYTNVG TSGLVAVNPH KYVPSNSDSV
     LQKYAAEYRD TTPSKVLLPP HIFQLANNAY YHMRRTAQDQ CILLSGETGS GKSENRRLAI
     KTLLDLSVNN PGKKGSKLAH QLPAAEFVLE SFGSARTLFN LNASRFGKYT ELQFTERGRL
     CGVKTIDYYL ERGRVASVPS GERNFHIFYY LMAGASPEER QHMHLNEKAT YRYLAQRTLP
     GRPTQGRDED ATRFDQLKMA LKNVGFSKRH VAQTCQLVAA ILHLGNLEFT IDRHRNEDAA
     VVRNMDVLEI VAEFLGVQPA ALETALTYRT RLMKKELCTV FLDPDGAADN RDELAVTLYS
     LLFTWLNEYI NQRLHKDDFT SFIALLDLPG PQNLTSRSNG LDQFCVNFAN ERLQNFIQKR
     LFESHVSEYN AEGISRFVPQ VPYFDNSECI RLLQHRPGGL IHIMDDQARR MPRKTNHTMV
     EAFAKRWGNH SSFKVGSADR SGFPTFTINH FTGPVTYSAE GFLEKNQDTM SPDFVQLLRG
     TSTNDTPATD GSGSINPFVR GLFTSKAIAT QMHPKNEETI IAAQQPVKPM RAPSTRRKNT
     VKRMSTLKEN EIDEKEEEEA PGAAPCIAGQ FRATLDMLFE TLEEAQAWYV FCISPNDSQL
     PNQLEGRSVK GQVRSLGLSE VARRCANMFE VAMTPQEFLE RYQDTLQQVG VHEGEPKEKV
     ERSRTALGLE EKDVVLGMTM AFLSHAAFHR LEDDLRAKDT EEQKRNKLRE AEAEAGLDPR
     GLSDPYAPYS TPGQEGPYEG GYNDPFGQSN QQLPLVSNAS PFHRGGGYED YDDQKSMDEY
     DVRSALTSHR DDESQSNFGT ESYAPSRNMF QAADKGLADK EAIAGEIQEG ETVETIKETS
     ARRRWVALCW LLTWWVPNPI LKWVGRMKRP DVRQAWREKL ALNMLIWLMC GAAVFIIAII
     GPLICPTEHV FSSSELQSHS FQNSPNNVYT SIRGEVFDLT QIAATHQRIV PVVPEKSILN
     YGGVAADNIF PVQVSALCNG VSGTVSPYVV LDSSNNTDPN AQYHDFRAWT TDPRPDWYFE
     SMTLMRWNNR VGFVGIDSKE LKNMANAQHS VAVYRGLIYD LTSYIANGPA VAAPKGEQTP
     SGIDTQFMDQ SVIDVFQFNA GQDVTKKIDN LNLPSNVLNW QRTCLRNLFL IGRVDNRNSP
     QCLFSQYILL ALSIMMVSVI GFKFIASINF TSARAPEDHD KFVICQVPCY TEGHASLRRT
     IDSLAQTKYD DKRKLLFIIC DGMVVGAGND QPTPRIVLDV LGANPNVDAE PLSFLSLGEG
     AKQHNMGKVF SGLYETRGHV VPYIVVVKCG KPGEKSRPGN RGKRDSQMLL MHFLNKVHFN
     TPMNPLELEM YHQIKNVIGV NPTFYEYLFM VDADTTVAPL ALNRLVSAMI HDKKLLGVCG
     ETELANAKQS IITMMQVYEY FISHHLAKAF ESLFGSVSCL PGCFTLYRLR TPDTHKPLLI
     SNQLIQDYSE NRVDTLHMKN LLHLGEDRYL TTLLLKHFSH FKTQFVRDAH AYTIAPDDWK
     VFLSQRRRWI NSTVHNLGEL VFIDELCGFC CFSMRFVVMI DLISTIIQPV TVAYIVYLIV
     LVAAEGKTIP TLSIVMLAAV YGLQALVFIM RRKWDMVGWM IFYILGIPVF SLFLPLYSFW
     RMDDFSWGQT RIVLGEAGKK MVVHDEGKFD PRSIPLKSWN DYENELWDKE SNHSIGSWVP
     PTKFQNDGYA ESQTASMYGR ETYYDPAMSH AYSPSPSQTG MAHPPPGYQS GRNTPMSMSY
     MPSVLHQPTP SRPATSYLDV QMPTSHSPED IDLPPGAPTD AEIDRAVQHI LQDADLTSVT
     KREIRRQLEE HFGMDLSSRK AAINAAIDRV LLERAG
//
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