ID L8FXB6_PSED2 Unreviewed; 1790 AA.
AC L8FXB6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=GMDG_07225 {ECO:0000313|EMBL:ELR05184.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR05184.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) 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}.
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DR EMBL; GL573376; ELR05184.1; -; Genomic_DNA.
DR RefSeq; XP_012745676.1; XM_012890222.1.
DR STRING; 658429.L8FXB6; -.
DR VEuPathDB; FungiDB:GMDG_07225; -.
DR HOGENOM; CLU_000192_0_0_1; -.
DR InParanoid; L8FXB6; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000011064; 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:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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; 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 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.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123};
KW Reference proteome {ECO:0000313|Proteomes:UP000011064};
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 745..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1051..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1442..1465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1477..1496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1503..1526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1731..1788
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1693..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1790 AA; 196007 MW; 0FD95BABA07B0968 CRC64;
MTNNNRHSIM SLGSMGGAIR GPPRNSPGQQ SSQVSTTTLL NALHNTYTSS QPYQLDASTS
LVVNTWLTAT QVDHNGGSGG VVDAALAARA WEHARRRAED GCIMLGYLHE SAPSVIVPFL
STLPLKMPAS LYTALNVLRP FTHAVTPQNG STPLHSALGV TLTLTLDGHL TGAALALSRG
GIDTARGLLN VPAAPGHRAF DVFYYLLTSA STAAEREFLG LKAPSTYALL SRSGTYDPPP
YVPTADDSAA AEDFRAGLKE IGIKGSAHRN LLSMLIGILK LGDSLSFNLD GDALEEVCED
IGGLLGLDPE LLASKCSTAE RETLVGALYE AVVDWVVSRA NSAIASEMLR IRNVDDSSDG
ERTPGTDEDS GDTVCITVLE VPGVALGKAA AMRGVFDDTQ GINAEMKEDG VDIVAAGSSV
LREMENAVSE VGPELGIMTG PPGRDREHAR DRREAVLEKV GREGEEDGFL KTIIFPVDGE
GVNLGRQGRL DLTTVLGSSR VWYHLSLHPV DDAPASLVSL PSTTSAWSAG TMSRQLRAWR
LPEWANRRTK NLDFTADFDH DEFAVRYASL GCKDGRDGVE SWVLERGWTN GEVVVGRERV
WMREGAWWEA ESMFDLTPTQ AGGEYGVLGD LLGAGGFESG YPAGGNDASG FFNAAPSELH
HQDSREGFLQ PGDGGARAKS VFGAQSKAPT RAQGAGDYGL GFKGDNTQGH VDYDNELGEF
VDNLDPELAN PRAVVTDKVT FSRRLWVGIV WALTFWIPSF MLRHVGRMKR PDVRMAWREK
VVLVFIIFLI NGIIVFYIVV FGRLLCPNFD KVWDTANVAT HQGDNDFWVS IHGKVYDISN
FWKQDHGTTS RPVRSSDMGQ LRGLNLDAYF MPPLTFSCPD VVTDPLVYVM QNGTQSAFSW
ALHDSGPFRD SSTTDKMHLQ DWYQATFLPR MKEYYKGHLV TKADLVKSDG SDNSHYWFII
DGAIYDLNNY FYTLHTMGGQ ALYDYLNPGF STMVKNNPGQ DLTGAYAQLL ATATSDAEST
SIKNSFNCVK NTFYIGIPDF RWTPRCQANN YILLAFTIIL CMVIGVKFLA ALQFGSKRRP
AAQDKFVVCQ VPAYTEGEES LRKALDSLTA LQYDNKRKLL CVICDGMIVG GGNDRPTPKI
VLDILGVDPK IDPPALPFHS VGQSGEQLNY GKVYSGLYEF EGNVVPYLVI VKVGKESEQS
KSKPGNRGKR DSQILLMSFL NRVHHRSPMN PLELEMFHQI NNIIGVDPEL YEYLFMVDAD
TSVREDSLNR LVAACANDAR IAGVCGETSL ENEEKSWWTM IQVYEYFISH HLAKAFESLF
GSVTCLPGCF TMYRLRTADK GKPLLISDAI VSEYADCDVD TLHKKNLLSL GEDRFLTTLM
TKHFPYMSYK FIPDAYASTA APDTWSVLLS QRRRWINSTI HNLAELVRLR EMCGFCCFSM
RFVVFIDLFG TIILPATCVY LVYLITTVAL GKSQFPLISI IMIACVYGLQ AIIFILKRQW
QHIGWMIIYI LAFPIYSFVL PVYSFWNQDN FTWGSTRIVI GESGDKRLVA IDDDGFDPRS
IPLQRWDDYA AANALPGRRA AGLEKLENPY DDAYEMDDFR SVYSSVKPAS TMGFGGGGGV
PGRRFIPPPL PSPYGAGQQG QVSRQSVFST SPYADQPQQV TRRPSMLSLG SPMENPYAAG
GARPNTIHVS TLPSSENLLG GMGSPSPGPG ARGNRNTIGY PMGGAGPAPG GPSDEAVVEA
IRACLADVDL DTVTKKQVRA LVEQRLGGGV GGVDRRAFVD RAIDGELANM
//
