UniProt: A0A366S0G6

Database: UniProt
Entry: A0A366S0G6_9HYPO

LinkDB:  A0A366S0G6_9HYPO 
Original site:  A0A366S0G6_9HYPO

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (3)   
   SMART (2)   
All databases (27)   

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ID   A0A366S0G6_9HYPO        Unreviewed;      1861 AA.
AC   A0A366S0G6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=FIESC28_04370 {ECO:0000313|EMBL:RBR22807.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR22807.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR22807.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR22807.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RBR22807.1}.
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DR   EMBL; QKXC01000084; RBR22807.1; -; Genomic_DNA.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000253153; Unassembled WGS sequence.
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; 1.20.58.530; -; 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; 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; 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   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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        883..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        923..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1200..1219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1589..1612
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1624..1643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1650..1673
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          946..1008
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          1803..1858
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1861 AA;  206961 MW;  2686A5A896158D7D CRC64;
     MSLPQLGGAG GPHTQPSLPS LPAHLQSDTH LTAHLASRFH VSHPTARLSS HALISLNTYT
     NSSKGPDGGK EGSAMAGAED IADRAFLRLG HRSENQAVVF LGESGAGKST IRAHLLTALL
     NKSSTPLSTK LSLAAYVFDS LTTTKTATTP TASKSGLFYE LQYDTSSTTN PVLIGGKLLD
     HRLERSRIAD VPTGERNFHV LYYLLAGTSE AEKSHLGLDG GSNAAGTTQK RWKYLGHPTQ
     LKVGINDAEG FQVFKNALRK LEFPRAEIAE ICQILASILH IGQLEFETTS QTSVTGDDSG
     GFSHEGGTTI TAVKNKDVLS IVAAFLGVSA ADLQTTLGYK TKMIHRERVT VMLDPNGARA
     HAGELARTLY SLLVAWILET INQRLCAPEE SIANTVSIVD FPGFCQQSPT GSALDQLLNN
     AATESIYNLT LQNFFDRKAD MLESEEVSVA ATSYFDNSDA VRGILKPGNG LLSILDDQTR
     RNRTDMQFLE ALRRRFDGKN AAIEVGSAQA KLPGSNFMTE NTSACFTVKH FAGEVDYPVK
     GLIEENSEVI SGDLLNMING TKSEFVARLF GQDALQTVTH PTERTTVMQA TVSSKPMRAP
     SVMSRKTHRT GRPSTAYKRQ QQEAMEELDQ QSQAGESKKN SKIVLEQGAS GQFLASLDNL
     QKAVTDPGTN SYFIFCLKPN DRRIANQFDS KCVRMQVQTF GIAEISQRLR SADFSLFLPF
     GEFLGLTDAE TILVGSERER AEMVIEEKQW PQNEVRVGAT GVFLSERCWM EIAQLGEVVS
     VGGRYGGLPS SDAGDGLTPA ESIPYGVSKE NLVSGGNTPL MYGEKAKGGY FTDDTRSEAG
     VSAFGGGDMF KNLDTREQMA ERGNEKSLEE VEEYRDKPSR KRWVALVFFL TWFIPDFAIR
     LIGRMPRKDV RMAWREKVAI NMLIWLMCAI AAFFMVGFPM LICPKQFVYS AGELSSYDGD
     KGSKGAYVAI RGFVIDLEKF IPNHYPGSDL VSENTLMKYA GKDITPLFPV QVSALCQGKD
     GAIPPEVTLD NRNTNITGQP QLLAQRDVDV NSIYHDFRYG TNDSRPDWYF EQMYTFKHVY
     LKGRMGYSPK YVEKLARDSA WNIVTIHGKV YDMTQYLKGG LRMKPKPGKD VPNIPGATEF
     MEDSVIQLFR SAKGQDVSKY WDNIKLSAVK KQRMETCLNN LFYIGDSDTR NSTRCQFAEY
     FILAISVMLA SILVFKFLAA LQFGGKNVPE NLDKFVMCMI PAYTEDEDSL RRAIDSLSRM
     KYDDKRKLLV VVCDGMIIGQ GNDRPTPRIV LDILGVSETV DPEPLSFEAL GEGMKQHNMG
     KIYSGLYEVQ GHIVPFMVIV KVGKPSEVSR PGNRGKRDSQ MVLMRFLNRV HYNLAMSPME
     LEMYHQIRNI IGVNPTFYEY LFQIDADTVV APDSATRMIS AFIDDTRLIA CCGETALTNA
     KGSFITMIQV YEYWISHNLS KAFESLFGSV TCLPGCFSMY RIRAAETGKP LFVSKEIVED
     YSTIRVDTLH MKNLLHLGED RYLTTLLLKY HSKYKTKYLY SAQAWTIAPD SWAVFLSQRR
     RWINSTVHNL AELIPLAELC GFCCFSMRFV VFVDLLSTIV QPVIVMYIVY LIYQVASNPS
     VVPITAFLLL GAIYGLQAII FILRRKWEMV GWMIMYIAAI PVFSFGLPLY SFWHMDDFNW
     GNTRVIAGES GKKIVVSDEG KFDPNSIPRK KWEEYQAELW ETQTQTARDD VRSEISGYSY
     ATKAQGPFSD YGGGYQPSRP GSTAGFGHQN MSRMSLAHSE MPGNRMSQFG GSQFFSPEEM
     VGMPSDDALL AEIRDILKTA DLMTVTKKGI KQELERRFNV PLDAKRAYIN SATEALLSGQ
     L
//

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