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Database: UniProt
Entry: A0A197JG90_9FUNG
LinkDB: A0A197JG90_9FUNG
Original site: A0A197JG90_9FUNG 
ID   A0A197JG90_9FUNG        Unreviewed;      1856 AA.
AC   A0A197JG90;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   31-JUL-2019, entry version 23.
DE   SubName: Full=Glycosyltransferase family 2 protein {ECO:0000313|EMBL:OAQ24140.1};
GN   ORFNames=K457DRAFT_82418 {ECO:0000313|EMBL:OAQ24140.1};
OS   Mortierella elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota;
OC   Mortierellomycotina; Mortierellomycetes; Mortierellales;
OC   Mortierellaceae; Mortierella.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ24140.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ24140.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ24140.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P.,
RA   Wu S., Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A.,
RA   Zienkiewicz K., Morin E., Tisserant E., Splivallo R., Hainaut M.,
RA   Henrissat B., Ohm R., Kuo A., Yan J., Lipzen A., Nolan M., Labutti K.,
RA   Barry K., Goldstein A., Labbe J., Schadt C., Tuskan G., Grigoriev I.,
RA   Martin F., Vilgalys R., Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis
RT   in the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV442100; OAQ24140.1; -; Genomic_DNA.
DR   EnsemblFungi; OAQ24140; OAQ24140; K457DRAFT_82418.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000078512; 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   Gene3D; 3.10.120.10; -; 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; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; PTHR22914; 2.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
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   ECO:0000256|SAAS:SAAS01194079};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078512};
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:UP000078512};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:OAQ24140.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1856       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008275907.
FT   TRANSMEM    841    858       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    878    898       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1146   1165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1541   1565       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1571   1589       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1596   1619       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    736       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      906    968       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND      14     21       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      156    177       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      534    574       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      603    625       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION      780    833       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    156    172       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    552    574       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1856 AA;  206934 MW;  4CA3D0E8D3B3E21B CRC64;
     MLVIITIFFC ICSGVSGSGK SVGASHITSQ LCRLATHTKK ESRVASQLQQ AQQILDAFGC
     AYTKDNQNAS MFSKFLEIQF NERGRILGGK TLCYLLNVSR ITKTPHHERT FHVFYYLLHA
     NQAAFSDQDK SQLRLQETFT YINQSRLARQ DTLGQGGLGA SSATSVPTPN SHAVPVSAGM
     GTDDTLGFEQ LKRAMSACGF KPRQTQHIWR LLAAILHLGN LQFSDPVSAS KQSTVQEAAA
     IRNPDILDLI ADILGVPSDK LMTALTYKSK LIRRDLCTVV LNSHGAIAHR DSLARALYMA
     LFGYLVEQIN KTLCHSEPAN FVAILDQPGL TEAPSSSAIH LANFEQFSVN FANELLHGFV
     GRRMLDDTVG FNKLQVQDGI QLPGPIQRAL PYSVRIQQQQ QQQQSGTTTA TSAVLGGLVR
     IMDDSSALFS QGTATDADCL HKATVQMRGD PQSQTIFSTN RTSSNYFAIQ HFTGKVEYSV
     DDFLEKNLDQ ISPDFLVLLR NSANRFIVDL FSVESAGAIS VERHPKFEKT IVKAQLQTRP
     KRQPSRQGRS LAARRGANTN KGSEIQQQQQ APQSVLSAMM QARQMEEDAV TVSTVLSQVF
     TTVHDLAQTM DETTLWHMVC LKPNDVQTNF SVDTKKMRNQ VNAFMLPEIA HRKRTEYTVS
     YVFSEFLSRY EKTTLLTNLA IDRTTKTEKG QCLEVANAPG RGWNAPDGKV GAKFALGNTC
     VWLAEEVWKD LEDDLRTVEK EERLRIKREQ AQALAMEEDD DMMSDYGMAS LSHNRILGRG
     SRRDQTLGAA TGGNGGQGGG EKGGNGRANQ AGVRKGQSGP SEKQQQKEPV EELPTTRARK
     LWVAFTWAMT WWIPSFMLSS CGKMKREDIR MAWREKVALC CIIFFMSAII IFVITGFGKM
     MCPGAEHLFS SKEVGYHASP DDFYVSLRGK VYDITKFAKN DHSNGHASYP SDTAYMLPFA
     GMDLTEYFPL QLNIACYGIV TSPTLSLVAN NTLIGAQLHG PPTSDTTIGW SQQNNQGQWY
     WKVALPRLQP MKKGELAFEM EDIKGDETRK WFVIDNAVYD MTSYFNTVRA PGNTGAQGAG
     VPSVHFLDKT VEDMAFNHNG EDVSDLWKKL PLDSQKRVLT KSCLDQVFYV GKVDYRKSFQ
     CQFTNYMLLS TSVVLVSVIA IKFLAALQLG SVRVPEEHDK FVIVQIPCYT EDEDSLRKTI
     DSITSLRYDD KRKLLFIICD GMIIGSGNDL PTPRIVLNIL GHDPSLDPEP LAFKSIGDGS
     KQMNMGKIYS GLYEHEGHVV PYIVVSKVGK PSERSRPGNR GKRDSQIILM KFLNKVHFDS
     PMCPLELEIY HQMKNVIGVN PSFYEYILQV DADTEVMPDA LNRLISCMIH DGKIIGLCGE
     TQLGNEENSW TTMIQVYEYY ISHHLAKAFE SLFGSVTCLP GCFCMYRVRT VAKSLPLIIS
     SKVIEEYSDN QVDTLHKKNL LSLGEDRYLT TLMMKHFPQY KMTFTPDATC KTVAPDRWSV
     LLSQRRRWIN STIHNLAELM FLPEMCGFCC FSMRFVVFLD LFGTLTLPAS VIYLVYLIVI
     VATGMETLPQ ISLILLGAVY GLQALIFIIK RQWQHIGWMF IYILAIPLFS FFIPVYSFWH
     FDDFSWGNTR MVVGETGSAK KVVILGDDEE PFDEKMIPMK KWSVYEQEMW EIDSVGSHES
     KGTVVSYRSK ISEQHGPGNG SSPMVMYNHA HRMSISSQPG VIPAMGMPGP VPYASSAVPS
     LRGGGSQYGS GSVVGAPLDI GYHTCGHGHG QQGHGHHMRT GSTASGSVAQ FVPPTMGSDQ
     PTDEELANEI QNVLATADLM SITKKQVRER LMAFFGVDLT SRKEYINEVI ERVLES
//
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