ID G4UKY8_NEUT9 Unreviewed; 1810 AA.
AC G4UKY8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=NEUTE2DRAFT_108303 {ECO:0000313|EMBL:EGZ73581.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ73581.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ73581.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891217; EGZ73581.1; -; Genomic_DNA.
DR STRING; 510952.G4UKY8; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_0_1; -.
DR OMA; WILERGW; -.
DR Proteomes; UP000008513; 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 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 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 SMART; SM01117; Cyt-b5; 1.
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.
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:UP000008513};
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 742..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1047..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1438..1461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1473..1492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1499..1522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 807..869
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1752..1808
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1810 AA; 201131 MW; 2CC71FC5ABE65CA3 CRC64;
MASDAGMGGR GPGQQQPSQV STTTLLNSVH NIYLSSQPYR LDAGTSLVVN TWLTASQAGP
DGHVGGTVDG ALALRAWEHA RRRAEDGCII LGSLHNSTPS LLRPFLFTIP LEIPASVYKA
LDAIEPFLRC VTPYNPSTPR QTGLAVTLTL NLTGNLTAAS LSLTQGGIDT DKGLLGVPSE
PGYRAFDVFY YLLTTASTPA EREFLGLKAA SQYSLLARSG TYDPPSYLPT ADDGAAADDF
RSALKDIGIK GSSHRNLISI LAGLLKLGNT LDYNVDQEVL EEICEDVGGL LGIEPEILAR
QLSTDDRATL IGGLYEALVD WVIKKANDAI AVQMGRSRNG DDSSDGASRS GAPTSNEDSG
DTVCLTVLEI PDQNLGKAIA MRGIFDDTQG INSEMKADGV EVVPVSSSVV REMQSAVAEC
GPDLGIMVGS VGRERQRLIE KREEILEKTA FASEDEGFLR KLLLPVPTEG INLGRTGRVD
VADLLNRSRA WYHLCIHPTD DSPSSLAALP AVNSAWSAGA VSRQLRTWRL SEWANRRNKH
IDYTADFDHH EFTQRYRPLG CMDGRDGIES WILERGWSNG EVVVGNERVW MRESAWWEAE
SMLDLKPMEA ERLNSMRNLM APGAMGSGYS HNGSGFFPPQ VHADHMRSPF ADGTSNGSYD
HLALGGNLSQ NNLNPSPVRA PSVAPTNMTG MRSGDYGLGP KGDQYKGQVF YNAEGQLVSE
LEPDLAEGKK IEERPISSQR KIWVFIVWAL TWWIPSPLLK FVGRMKRPDV RMAWREKFVL
CLIIVILNAI IVFWIIFFGR LLCPNFDKAW TLEEIQNHAA GDDFWVSIDG KVYDITKFWR
LQHSDNNIDT SSDVMMPLAG QDLSAYFVAP LYISCPGLGI ADSTTLQFNT TPEYVVAQHI
SGPTQPNIRS KLSERYWYTE RFLPAIKEYY HGDVVWDSKK IKQEGLDWNH PWFIYEDLVY
DMTDYMYTAK RMNNDATYTF IDAKITNMVK NNPGQDLTEQ INDLIDRASS NQTQYESVMN
SLNCVKNTFY VGKPDFRYSA RCQVNNYILL AFSIIICSII VVKFVSALQF GSKRRPAPQD
KFVICQVPAY TEGEDSLRKA LDSLTALQYD NKRKLIFVIC DGVIVGAGND RPTPKIVLDI
LGVDPKVDPP ALAFKSVGTG AEQLNYGKVY SGLYEFEGNV VPYIVVVKVG KESEQSKTKP
GNRGKRDSQI LLMSFLNRVH HRAPMNPLEL EIFHQINNII GVDPELYEYL LMVDADTCVR
EDSLNRLVAA CANNAKIAGI CGETSLQNED LSWWTMIQVY EYYISHHLAK AFESLFGSVT
CLPGCFTMYR LRTVDKGKPL IISDDIIREY SDCYVDTLHK KNLLSLGEDR FLTTLMTKHF
PYMSYKFIPD AYCQTAAPET WSVLLSQRRR WINSTIHNLA ELIFLDEMCG FCFFSMRIVV
FIDLFGTIIL PATCVYIVYL IYTASSHTGP FPLLSIIMIA AVYGLQALIF ILKRQWQHVG
WMIIYLLAFP IYSFILPIYS FWHQDDFAWG NTRVVIGESG KKQVVAVDEE GFNPRAIPLQ
RWDEYALANN LPGRRGGPLE KGMDEHLGGM YEETYEVDDM KSVYSSVRQP SVLTGFGGRG
AGAYMPPHSP GFPPNGGGSG AMTHASTFVG ASPFTEQNNL MNRQSMASMG TMVEMQRRAS
PYQDFPGGHS RGPSQGAMRS MTNTPPALGA GGMVNARLST ATGMSLGIPG HRPGMSHSES
SRSFDFQRST PGPDDQMIIE AIQGVLREVD LDTVTKKQVR ALVEQRLQTE LVGERRTFMD
RQIDNELANM
//
