ID A0A397GND4_9EURO Unreviewed; 1758 AA.
AC A0A397GND4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=CDV56_106826 {ECO:0000313|EMBL:RHZ51034.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ51034.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ51034.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ51034.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-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: 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 -!- 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:RHZ51034.1}.
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DR EMBL; NKHU02000152; RHZ51034.1; -; Genomic_DNA.
DR STRING; 41047.A0A397GND4; -.
DR VEuPathDB; FungiDB:CDV56_106826; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
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 CDD; cd04190; Chitin_synth_C; 1.
DR Gene3D; 1.10.10.820; -; 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; 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; 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 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.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
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 728..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 764..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1025..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1451..1470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1477..1500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1700..1756
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1758 AA; 195875 MW; CD0CD8EE5D321713 CRC64;
MSNRFSVYSS HSAGFSTSGS RSAPQTTQVS TTTLLNALHA FYNSGQSYQL DAGTSLVVNS
WATASHTTPD GRTGGIIDRE LAIRAWEHAR RRAEDGCIVL CSAHQSTPSL LEPFLAALPL
PTPSIAFTAL AALRPFLSAV TAFNPSYSLY SALAASYTFT LQGSLVGLTF ALSTSGINVR
KGLLDISSEP GYRAFDVFYY LLTSTSTPAE REFLALKDTS AYTLLNKSGT YSPPAYLPTA
DDAAAAEDFR ASLKAIGIKG ASQRGLLSIL AGLLKLGNAA GFLVDQEELE EVCDEVGGLL
GLDPDVLLHK CSTEDREVLI AGIYEALVDW VITKANESIA NELRANQEGD SGSGSAGQWS
DEDTVGITVV DIPRPAFGKA VALRGIFDDT LGINAEMKED GVQIPPIGHS VLNDLNSSVA
QVEPDLGINT GPAWREREYE LDKRQEVLEK VGLEVDMDSF LRQLLFPVEA EGITVGKRGR
FDLMTTLGSS RVWHHISIHP TDDTPDSLNA ASPTAAWSAG AVSRQIREWR LAEWANRRLK
QMDFTADFDV EEFVSRYSRL GCREGRDGVE SWLMERGWTN GDAFVGRQRI WMRENAWWEA
ETMLDLKPDE TPGANSYMYG SGMLDTGMAQ YAANPMAESA SLLGSRDNLQ RQSMLAPSVG
GGAKSIAPSM PNTLNMAGDY GLGTKGDTKK WDNQLYDGDD GRYTGELDPE FGSPKHIEKK
EITFGRRVWA GFVWAMTFWI PSFVLRYIGR MKRPDVRMAW REKLVLVFLI LLFNAIVCFY
IMAFGDLLCP NKDKVWNSKE VGYHQGDNDF YVSIHGKVYD ISKFWKIPHG DSAGESTTST
MEPFMGQNLD AYFPPPLTRF CSPMVTDQSI TLSNNDTNAI LYSYAKHDCG PLTHASTTTA
LHNITWYEDT FLPKIREYYK GDLVWTRGTV AKQAENSQRY WVIVNQNIYD LTDYFYTLDT
MNDLDTYNFL PSSVTDLFKS YPGTDVTDKW QDTEDFKKSQ ICLDYVFYKG KVDFRDTPRC
TVNNWILLAF TVLICSVILV KFLAALQLGS KRRPAPQDKF VICLVPAYTE GEDALRKGLD
SLTALQYDNK RKLIFVICDG MIVGGGNDRP TPKIVLDILG VDPKIDPPAL PVKSLGQGSD
QLNYGKVYSG LYEYEGNVVP YIVVVKVGKE SEQNRPKPGN RGKRDSQILL LNFLNRVHHR
SPMSPLELEM FHQINNIIGV DPELYEYCLM VDADTSVRED SLNRLVAACA NDARIAGICG
ETSLQNEERS WWTMIQVYEY YISHHLAKAF ESLFGSVTCL PGCFCMYRLR TADKGRPLII
SDQVIREYAD NDIDTLHKKN LLSLGEDRFL TTLMTKHFPT MSYKFIPDAY ASTAAPETWS
VLLSQRRRWI NSTVHNLVEL AALKDLCGFC CFSMRFVVLV DLIGTVILPA TCVYIGYLIY
RVASNTGPFP YISLAILAGV YGLQAIIFIV KRQWQHVGWM IIYIMAFPIY NFILPLYAFW
KQDDFSWGST RIVLGEKGSK RVVAVEDEVF DPRSIPLQRW DDYALANNLP GRRGDYGVSQ
EKMYSRYGDE AVMEMDDLHS NYSSVKPAST ILTGFPQGRH SSPYMPPQSP APFGGNIPGN
RNSHLSSFTR YTDNPHQRNM SMGNLSHYQD SPMGMSRHSV GLMQSTDNLL GARQNSRSPL
GGGMNSRPVS AFDFRTGGTG PDEGAITEAI RSCLAEVDLD TVTKKQVRAL VEQRLQTTLT
GDKKAFLDRQ IDHELANM
//
