UniProt: V5FKV6

Database: UniProt
Entry: V5FKV6_BYSSN

LinkDB:  V5FKV6_BYSSN 
Original site:  V5FKV6_BYSSN

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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)   
Literature (1)   
   PubMed (1)   
All databases (28)   

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ID   V5FKV6_BYSSN            Unreviewed;      1854 AA.
AC   V5FKV6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=PVAR5_1009 {ECO:0000313|EMBL:GAD92418.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92418.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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:GAD92418.1}.
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DR   EMBL; BAUL01000025; GAD92418.1; -; Genomic_DNA.
DR   eggNOG; KOG2571; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   HOGENOM; CLU_000192_0_2_1; -.
DR   InParanoid; V5FKV6; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000018001; 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; 1.10.10.820; -; 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; 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   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:UP000018001};
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        895..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        935..954
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1203..1225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1601..1622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1628..1649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1656..1679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..789
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          958..1017
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          1796..1851
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..656
FT                   /note="Disordered"
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   1854 AA;  205817 MW;  25AC0D2564BA30C3 CRC64;
     MASHSFPGSA PSHAQSSLPS LPAHLQSDTH LTAHLASRFH VSLPTARLSS QALICLNTYT
     SSAKGPDGGK EGSAMGEAED LARRAWTRLG ARGENQAIVF LGESGAGKTT IRSHLLSSFL
     SFSSTPLSTK LSLAAFVFDS LTTTKTVTTP TASKAGLFFE LQYDGSSSTN PTLIGGKIID
     HRLERSRIAA VPTGERSFHV LYYLLAGTSA AEKAHLGFDN SVNINTGGTG NLSSGTVKHK
     RWRYLGHPTQ LKVGINDAEG FQHFKTALRK LEFPRSDIAE ICQVLACILH LGQLEFTTGQ
     ATTTAAEESG GYSHEGGETV TVVKNKNALE IVAAFLGLSM YDLETSLGYK TKTIHRERVT
     VMLDPQGARA NADELARTLY SLLVAYVIEN VNQRICAAED SVANTVSIVD FPGFAQVAST
     GSTLDQLLSN AATECLYNYC LQSFFDRKAD ALEREEVSVA ATSYFDNTDA VRGLLKSGNG
     LLSILDDQTR RGRGDAQFLE SLRKRFENKN PSIVVGSASS VMPGSNFVSP NAAAAFTVKH
     FAGEVDYPVD GLVEANGDIV PGDLMNLINS TKSDFVRSLF GQEALQTITH PKEKTAIMQA
     QVSSKPQRMP SLARRKVSPP RLSSMGTRIS EEAEDSSHAG SMTKSGAGRR KGTMLSPNQG
     AAGQFLASLD IINKSLSAPN VNPYFVFCLK PNDRRIANQF DSKCVRAQVQ TFGIAEISQR
     LRNADFSVFL PFAEFLGLAE VDTVVVGSDR EKAEAVLSER RWPGNEARVG STGVFLSERC
     WADLAKVGER VVPVYGADGI DDDAVYPAHG PYADSKVRLL NPAEQSPGAY IYGDETKQGY
     FGSRELDGRS DAGASAFNHD MFQNLETREQ MAEKGNERNM EEVEDVHVSA SRKRWLAIVY
     ILTFWIPDFL IRFVGRMKRK DIRVAWREKL AINMIIWFSC GLAIFIIVWF PGLICPTQHV
     YASSELASHN GKNGHSSFVA IRGVVFDLGE FMPSHYPNIV PQSALKKYAG TDATALFPVQ
     VSALCQGKTG TIDPTVLLDY SPTNVTDSGT AISGTDVNSQ YHDFRYFTND SRPDWYIEQM
     MMLRANYQKG YVAYSEQYMK TLADKKSTYV ASIDGSVFDF TSYVAGGRRT QAPVGKSVPK
     NVDTDFMEPT VVQLFQERAG QDVTKYWQNL DLDPVLRDRM WRCMNNLFFV GHVDTRNSPR
     CQFAQYFLLA ISITLCSVIT FKFFAALQFG KKNVPENLDK FIICQVPAYT EDEESLRRAI
     DSMARMKYDD KRKLLLVVCD GMIIGQGNDR PTPRIVLDIL GVPDNVDPEP LSFESLGEGL
     KQHNMAKVYS GLYEVQGHIV PFLVVVKVGK PSEVSRPGNR GKRDSQMVLM RFLNRVHYNL
     PMSPMELEMH HQIRNIIGVN PTFYEFILQV DADTVVAQDA ATRFVSSFID DTRLIGLCGE
     TALTNAKSSI VTMIQVYEYY ISHNLTKAFE SLFGSVTCLP GCFSMYRIRT AETAKPLFVS
     KEIVTAYSEI RVDTLHMKNL LHLGEDRYLT TLLMKHHPSF KTKFISSARA WTIAPDSWTV
     FLSQRRRWIN STVHNLVELI PLQQLCGFCC FSMRFIVFVD LLSTVIMPVT VAYIIYLIVW
     LVKDTSSIPF TAFILLGAIY GLQGIIFILK RKWEMVGWML VYILAMPVFS LALPLYAFWH
     MDDFSWGNTR VVTGEKGRKV VLSDEGKFDP SSIPKKKWEE YQAELWEAQT SRDDRSEISG
     FSYGTKSYHP AQSEYGFPGS RPMSQMDLPR FGSRMSLAAS EMMGRRDMEM EDLAGLPSDD
     TVLAEIREIL RNADLMTVTK KSVKQELERR FGVNLDSKRP YINSATEAIL SGQL
//

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