UniProt: A0A151GRE2

Database: UniProt
Entry: A0A151GRE2_9HYPO

LinkDB:  A0A151GRE2_9HYPO 
Original site:  A0A151GRE2_9HYPO

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A0A151GRE2_9HYPO        Unreviewed;      1859 AA.
AC   A0A151GRE2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=DCS_00828 {ECO:0000313|EMBL:KYK59694.1};
OS   Drechmeria coniospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX   NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK59694.1, ECO:0000313|Proteomes:UP000076580};
RN   [1] {ECO:0000313|EMBL:KYK59694.1, ECO:0000313|Proteomes:UP000076580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK59694.1,
RC   ECO:0000313|Proteomes:UP000076580};
RX   PubMed=26975455; DOI=10.1038/srep23122;
RA   Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA   Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA   Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA   Molnar I., Lin M.;
RT   "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT   Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL   Sci. Rep. 6:23122-23122(2016).
CC   -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC       septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC       reducing end of the growing chitin polymer.
CC       {ECO:0000256|ARBA:ARBA00024009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC         D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC         UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223; EC=2.4.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00000319};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYK59694.1}.
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DR   EMBL; LAYC01000001; KYK59694.1; -; Genomic_DNA.
DR   STRING; 98403.A0A151GRE2; -.
DR   InParanoid; A0A151GRE2; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000076580; Chromosome 01.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 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; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51998; DEK_C; 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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        882..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        921..941
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1587..1607
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1613..1635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1642..1665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..777
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1801..1856
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         105..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1859 AA;  205318 MW;  CD1BE0C74F6F4BF2 CRC64;
     MATTISSQGA GNGGAHSQHS LPSLPAHLQS DTHITGHLAS RFHVSQPTAN LSSHGLVCLN
     TYTSSTKGSD GGKVGSAQAG AEDMANRAWQ RLGHRSESQA IVFLGESGSG KSTVRHHFLA
     ALLNKSSTPL ATKLSLAAYV FDTLTTTKTA TTPTASKSGL FYELQYDTTG STNPVLIGGK
     LLDHRLERSR ITDVPSGERN FHALYYLLAG TSEAEKAHLG LDASKRWKYL GHPTQLKIGI
     NDAEGFQLFK NALRKLEFPR ADIAEICQVL ASILHIGQLE FETTSNTSAT ADDSGGFSHE
     GGTVTTTVKN KDVLAIIAAF LGVSTGDLQT TLGYKTKTLQ KERVTVMLDP NGARAHANEL
     ARTLYSLLVA WIIENANQRI CALEDGVANT ISLVDFPGFA QQSSTKSALD QLLNNAATEA
     IYNMTLRNFF DRKADMLESE EIRVAPTSYF DNSDAVKGLL KPGNGLLSIL DDQTRRSRTD
     MQLLDSLRKR FEGKNPAIEV SSATAKLPGS NFLTENTTAS FTVKHFAGEV DYPVKGLIEE
     NGEIISVDLL NMFNSTKSEF VGRLFGQDAL QTIAHPTERA AVLQATVSSK PMRAPSVMSR
     KGGRAAAAHR RQQQEAAEQL DQASDTKSSK NGGGRGVAAE QGASGASGQF LASLDNVQKA
     VTDPGTNTYY VFCLKPNDRR IANQFDSKCV RTQVQTFGIA EISQRLRSAD FSLFLPFGEF
     LGMANAETII VGSERERAEM FIDQKRWPVN EVQIGATGVF LSERCWMEVA QLGEKGEQRA
     GLSTDSDGGD GQTPGFPQHA FGVSKEELLL SGGGTPLMYS EKGGKGYFGG SDDTRSEAGV
     SAFGGGDMFK NMDTREQMAE RGNEKSLVEV EEFKDSPSRK RWVFTVYLLT WLIPDFLIRW
     FGRMPRKDVR MAWREKLAIN ILIWILCLVA AFFIIGFPML ICPKQNVFST EELSSKDGKG
     GSPAYASLRG YVIDLGQYAS HHYPPFLEAK NLLNYAGKDI STLFPVQVSA LCQGVSGSID
     PAVTLEYRNT SETSNLPLTV RIQDINAQYH DFRHFTNDSR PDWYIEQLMM LRGTWGAGKI
     GYTPEYVAKL GSKQQRIAII GGKVYDMTTY FSGGRKMIAK PGEKPPTDTT LTDFMHPDVV
     SLFLYGSGTD ITKSWEALNP TIKPGMRTCL DNLFYIGDVD TRNSTRCQFA EYLVLGVSIL
     LASVIAFKFF AALQFGGKNL PENLDKFVLC QIPAYTEDED SLRRAIDSAA RMRYDDKRKL
     LVIVCDGMII GQGNDRSTPR IVLDILGVSE TVDPEALSFE SLGEGQKQHN MGKVYSGLYE
     VQGHIVPFMV IVKVGKPTEV VRPGNRGKRD SQMIIMRFLN RVHYNLAMSP LELEMYHQIR
     NIIGVNPTFY EFMFQIDADT VVAPDSATRM VSAFLDDTRL IACCGETALT NAKSSFITMI
     QVYEYYISHN LSKAFESLFG SVTCLPGCFS MYRIRAAETG KPLFVSREVV ESYATIRVDT
     LHMKNLLHLG EDRYLTTLLL KYHSKYKTKY LFSAHAWTIA PDSWAVFLSQ RRRWINSTVH
     NLMELIPMNQ LCGFCCFSMR FIVFIDLLST VVQPVTIGYI VYLIVLVSTK ATVVPITAFV
     LLGAIYGLQA IIFILRRKWE MVGWMILYVL AIPVFSFGLP LYAFWHMDDF NWGNTRVVAG
     ENGKKVVITD EGKFDPSSIP RKKWEEYQAE LWETQTSRDD ARSEVSGFSY GTKAHALVSE
     YAFPSRPNST AGFAAQPSMA HLPYDSRNAS RMSLAASDMG ANRMSHFGGS QFFSPEDMVG
     LPSDDALLAE IRDILKTADL MSVTKKGVKQ ELERRFDVPL DAKRAYINSA TEALLSGQL
//

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