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Database: UniProt
Entry: A0A0F7VE98_9EURO
LinkDB: A0A0F7VE98_9EURO
Original site: A0A0F7VE98_9EURO 
ID   A0A0F7VE98_9EURO        Unreviewed;      1862 AA.
AC   A0A0F7VE98;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   31-JUL-2019, entry version 22.
DE   SubName: Full=Putative Chitin synthase V {ECO:0000313|EMBL:CEO60363.1};
GN   ORFNames=PMG11_04992 {ECO:0000313|EMBL:CEO60363.1};
OS   Penicillium brasilianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=104259 {ECO:0000313|EMBL:CEO60363.1, ECO:0000313|Proteomes:UP000042958};
RN   [1] {ECO:0000313|EMBL:CEO60363.1, ECO:0000313|Proteomes:UP000042958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; CDHK01000004; CEO60363.1; -; Genomic_DNA.
DR   EnsemblFungi; CEO60363; CEO60363; PMG11_04992.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000042958; 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   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; 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   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   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Complete proteome {ECO:0000313|Proteomes:UP000042958};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000042958};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    894    913       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    934    953       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1203   1225       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1601   1622       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1628   1648       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1660   1679       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    786       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      957   1016       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND     101    108       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION        1     21       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      596    654       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    606    637       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1862 AA;  207317 MW;  579EB2256B106F1D CRC64;
     MAGNNTGSTP AHAQSSLPSL PAHLQSDTHL TAHLASRFHV GLPTARLSSQ ALISLNTYTS
     ATKGPDGGKE GSAAGEAEDL ARRAFTRLGA RAENQAVVFL GESGSGKTTI RSHLLSSFLS
     FSSTPLSSKL SYAAFVFDTL TTTKSVTTPT ASKAGLFLEL QYDGSSSVNP TLIGGKIIDY
     RLERSRISSV PTGERSFHVL YYLLAGTSAA EKSHLGFDNS IHISTGGGKL SSDSVTSKRW
     RYLGHPTQLK VGVNDHEGFQ HFKTALRKLE FSRGEIAEIC QILASILHIG QLDFVSGQST
     TTTAEESGGY SHEGGEMVTV VKNKDALGNV AAFLGLSVES LENSLGYKTK TIHRERVTVM
     LDPRGARENA DAFARTIYSL LVTYVIETVN QKICAAEDSV ANTISIVDFP GFAQAPATGS
     TLDQLLSNAA TESLYNYCLQ SFFDHKADVL DREEIAVAAT SYFDNTDTVR GLLKHGNGLL
     SILDDQTRRG RSDAQFLESV RKRFEGKNPA ISVGSGGTTS SGYLSQARTA FTVKHFAGEV
     DYSVTGLIEE NGEVISGDLM NLMKSTRSDF VRELFGQEAL QTISHPREKT AIMQAQVSSK
     PLRMPSMARR KHDQQARQMF SDRGESEEPD DRDSQAASSR RSVAGRKSGL MTGPAQGAAG
     QFLSGLEIIN KCLSSPNLNP YFVICLKPND RRIANQFDSK CVRMQVQTFG IAEISSRLRN
     ADFSVFLPFA EFLGLAEIGN VVVGSDREKS EVVLDERRWP GNEARVGSTG VFLSERCWAD
     LAKIGERVVP SYNKISGSDE GDVGYNAGGA DTKVRLLNPT VQSPGAFIYG DESKQGGYFG
     SRELDGKSDA GASAFNSGDM FKNLETREEM LQKGNEKNME EVDDVVVSGS RKRWMALVYL
     LTFFIPDFLI KWVGRMKRKD VRVAWREKLA INMIIWFACG VAVFMIVAFP GLVCPTQHVY
     SKGELSNNNG KDGASSYIAI RGVVFNLGDF MPSHYPDIVP QKSLKNYAGT DATNLFPVQV
     SALCQGVDGH VDPSVPLDYR SNMNESSTTT STTDYDLNAK YHDFRYWTED YRADWFYEQM
     VMMRANYKKG YVGYTAKYMK TLADDDSKNI VSIDGKVYDM TYYIAGPRIP RYPTGKNASS
     NVNTNYMNSL LVTLFQQKSG TDVTKYWNDL AIDATTRSRM QLCLDNLFFV GHVDTRNSAR
     CQFARYFILA ISIMICMVIL FKFLAALQFG KKNLPENLDK FIICQVPAYT EDEDSLRRAI
     DSMARMHYDD KRKLLLVICD GMIIGQGNDR PTPRIVLDIL GVPESVDPEP LSFESLGEGM
     KQHNMAKIYS GLYEVQGHIV PYLVVVKVGK PSEVSRPGNR GKRDSQMVLM RFLNRVHYNL
     PMSPMELEMH HQIRNIIGVN PTFYEYILQV DADTVVAQDT GTRFVSAFLS DTRLIAACGE
     TSLSNAKTSI ITMIQVYEYY ISHNLTKAFE SLFGSVTCLP GCFSMYRVRS AESGKPLFVS
     KEVVESYSEI RVDTLHMKNL LHLGEDRYLT TLLLKHHPKF KTKYIFRCHA WTVAPESFAV
     FLSQRRRWIN STVHNLIELI PLQQLCGFCC FSMRFIVFVD LLSTIIQPVT VAYIIYLIVW
     LVRDTSVIPW TAFVLLGVIY GLQAFIFIMR RKWEMIGWMF IYILAIPVFT LALPLYSFWN
     MDDFTWGNTR VITGEKGRKV VISDEGKFDP ASIPKKRWEE YQMELWEAQE GQTSRDDHSE
     VSGYSYGTRA HPFAQSEYGF PGSRPVSQLD LPLLASGSRM SVAPSEMMSH HMDMDMSMED
     LSHLPSDDAI LAEIREILRT ADLMSVTKKS IKQELERRFG VNLDLKRPYI NSATEAVLSG
     LL
//
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