UniProt: F8PWN4

Database: UniProt
Entry: F8PWN4_SERL3

LinkDB:  F8PWN4_SERL3 
Original site:  F8PWN4_SERL3

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   F8PWN4_SERL3            Unreviewed;      1901 AA.
AC   F8PWN4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   28-JUN-2023, entry version 57.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=SERLA73DRAFT_168131 {ECO:0000313|EMBL:EGO00358.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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}.
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DR   EMBL; GL945479; EGO00358.1; -; Genomic_DNA.
DR   STRING; 936435.F8PWN4; -.
DR   eggNOG; KOG0162; Eukaryota.
DR   eggNOG; KOG2571; Eukaryota.
DR   HOGENOM; CLU_000192_0_0_1; -.
DR   InParanoid; F8PWN4; -.
DR   OMA; DYWISIR; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000008063; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04190; Chitin_synth_C; 1.
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:SF13; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 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; 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; PS50255; CYTOCHROME_B5_2; 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   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:UP000008063};
KW   Transferase {ECO:0000313|EMBL:EGO00358.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        861..878
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        899..921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1552..1576
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1583..1606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1612..1636
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..663
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          926..988
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          1843..1899
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          736..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1731..1767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1901 AA;  211847 MW;  9CEDE169592FF729 CRC64;
     MASSSATLLA QAVASASATV YPSDDALLSV LSARFRADLP YTRIGSSNLV VVNPYKTLSS
     VNDASAKEYE ERCYKDTKLA LVDSRKSVQP HVYELAARIY LLMRRRNESQ AVIPRGITGS
     GKSTNNRLLI EQILRLSAHS KKELKIVEQI KSLNVLLESF GNAKTPTNPN ASRHTRYTEL
     HFNSRGRISS AKALAYSLDK SRLTRLTHDE RSFHVFYQLL AGATHFERDD LGLDSPSDYA
     LLASSGCYRL PAGPFSDDGM AMEDLRAAMR SLGFKPKHTS SIFTVLTAIL FLTNIQFGEA
     DAQDVSAYVL NVPVLQHIAR LLGVDTDELG ESLTCKTTYV RKELYTVLLN VQQSEAQRDQ
     LVRDLYAILF AFVVETANHK LASNVKEQAP SSQIVLLDQP GFQSRASTGT TSMAAPPLIS
     THQNGFDEFC INFSDEIVQA HVLNSIFENE AGYNARAVAD GVSLPGVAVM DNSACAELIR
     GPQPNARKPG GLLGATGKAA SAFKSGKTGE QRNDDLLQDL RNDDLLQDLV SKFGVHASFI
     AGPSSAEERR SFGVNHYAGP VSYDVSSFVE KDADLLDPAF VSLLRSSSDP FVSKLVSGPS
     LATEKHQSDD GTIVQAQVSS RPLRLPTPIS SIPDENQRLN PTKIYPVTTQ IHQTLTDVLS
     TLSHAPRRSI EYVAEFEKAE FCDRYVPTMR GLEADRIRQC IQSNGWREGT DYALGNQNVW
     LSYRAWKMVE DVVRSAEKDQ KKNSREDSEE DESIFPDDTT EYNNGAAEQQ QRNYFDGPPG
     PVYEEPETPF DGYSSSHVVP ATPAMLPSPY RPYADDTGSE WDKKGDSFDG APPLIPKEGV
     MTVNEAPNVV EEIPSTRTRR VWLHIVRAFT WFIPSFLLSS LGRMKRPDVQ LAWREKMTIF
     ALITLANGIV LFYIIVFGRL LCPNFDKAWA SNEVAQHTGT NDFYVSIQGK VYDVSNFVQG
     DHSDITGEAS NGAATLEYLA GQDLTYYFPP PLVLACSGLV TDATMEIAIK NTSDIYVTQA
     VHNSGKNALV ATSALANEDW YTATYLPKIN QYYKGALVWE PSEISAQASD QTIQRIWGIY
     DSSIYDLTDY VYTQSTLEQN NAAYSFLDSS LVAVFNEQAG QDITSSLNQV LDAMDANTRS
     ANMDCLQNAF YWGETDFRYT PRCQVQNVLL LVFSSILMAS MGIKCKCHFC FPELLDKFVL
     CQVPCYTEGE DSLRRTIDSL AALDYDDKRK LIFIICDGNI IGSGNERPTP RIVLDILGVD
     PSHDPEPLMF RSIGDGAQKL NYGKVYSGLY EFEGHVVPYM VVVKVGKPTE RSKPGNRGKR
     DSQILLMQYL NRVHFNAAMS PLELEIYHQM RNVIGIDPAF YEYIFTVDAD TCVTPESLNR
     LVAAAADDSN IIGVCGETKL QNEEGSWWTM IQVYEYYISH HLSKAFESLF GSVSCLPGCF
     SLYRIRTADK GRPIFISNRI IDEYSENNVD TLHKKNLFSL GEDRFLTTLL MKHFPTYKTK
     FIPDALSRTM APVSWRVLFS QRRRWINSTV HNLCELAILA DLCGVCCFSM RFFVFIDLIG
     TIILPATVVY LLYLIITVAT GQGIFPLISI IMIAVVYGLQ ALIFILKREF MLIGWMVVYL
     ISYPIYSFFL PIYSFWCMDE FGWGNTRVVL DDGGNKKVIT NVDTRFNENM IPYKKFSEYE
     AETWDGGSRH TPEMETVHSH MAPSLHHNNG YGYSSSEAGD YYRDTNMTMN NSSKANLRVP
     SHRPSPSSRS TSEFPQRYPN TSPFMSSQER LTMHTPPAPY PGLGSVYGMP PPGSRMTMAT
     NMSAFNRGAS PALGAPPTLG ALRPTSTFSM ATTVFAGPNM NPNPSDEELY TALRNYLSTQ
     DLMTVTKKTA REAMTARFPK ADLVSRRDFL NQSIDNILSH S
//

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