ID G9NN49_HYPAI Unreviewed; 1857 AA.
AC G9NN49;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=TRIATDRAFT_142365 {ECO:0000313|EMBL:EHK48324.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK48324.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK48324.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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}.
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:EHK48324.1}.
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DR EMBL; ABDG02000019; EHK48324.1; -; Genomic_DNA.
DR RefSeq; XP_013946482.1; XM_014091007.1.
DR STRING; 452589.G9NN49; -.
DR GeneID; 25775687; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000005426; 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; 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; 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; 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:UP000005426};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHK48324.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 880..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1193..1212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1582..1605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1617..1636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1643..1666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..773
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1799..1854
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1857 AA; 205724 MW; 3C26E43191B69FE5 CRC64;
MSLPIGAAGN GGAHTQHSLP ALPTHQQSDT QITAHLASRF HVNLPTTYLS SHGVVALNTY
TSSVKGPDGG REGSAMAAAE DVADRAWLRL GNRSENQAIS FLGESGAGKS TIRNHIVAAF
LRKSSTPLST KASHAVYVFD SLTTTKTATT PNASRAGLFL ELQYDTSAST HPTLLGAKLL
DHRLERSRIT DVPTGERNYH VLYYLQAGTS DAEKAHLGFD NENGSKRWKF LGHPTQLRVG
INDADGFQLF KTALRKLEFT KSDIAETCQL LATVLHIGQL EFEVSNNTSV TGDDSGGFSH
EGGNTVTAVK NKDVLAIIAA FLGVSAADLQ TTLGYKTKVI HKERVTVMLD PNGARAHANE
LARTLYALLV AWIVESMNQR LCAPEENIAN TISIVDFPGF AQQAATGSAL DQLLTNAATE
AIYNMTLRNF FDRKAEMYET EEVTVSATSY FDNTDAVKGL LKPGNGLLSI LDDQTRRNRT
DLQLLESLRK RFEGKNPAIE VGSATAKLPG SNFHTENLAA SFTVKHFAGE VEYPVRGLIE
ENGEIISGDL MNMMNNTKSD FVAKLFGQEA LQTVTHPQER TTVVQATISS KPMRAPSVMV
RKGARPKLNA GGRRQTQDNF DSMSQDSDSR EPKRGAPKGG SEQGASGQFL SSLENVQKAI
SDAGTNAYFF FCLKPNDRRI ANQFDSKCVR TQVQTFGIAE ISQRLRSADF SLFVPFGEFL
GMANSEALLV GSERERAEAA IDERQWPRNE VSVGATGVFL SERCWLEIAQ LSFASGGSGR
GAMSAFDSEG GDGLTPGDHH AFGASKERLL SAGQTPLGYG EKGRSGYFGD DARSEAGASA
FGTGDMFKNH DTRAQMAERG NEKSMVEVEE YKDSSSRKRW LFVVYALTWF IPDFLIRLLG
RMPRKDIRIA WREKFAINLL IWFCCLVAVF FTAIFPILIC PTQHVYSAAE LSSYDGKSHS
NGAYTAIRGI VIDLGAFIPS HYPQGLVKQE TLEKYAGLDI TSLFPVQVSA LCDGVDGAID
PSVTLDYKTT NFSGSPALIS NTDANAKFHD FRAFTNVSQP DWFYEQMYYL KSRFKKGNIG
YTAKYVSSQG KNSQNIAILN SKVYDLTTYL AGGRHLRVKP GQPQPTNQSL TDFMDSSVTS
LFQLNPGQDI TKYWNSLRLD ATGKARMKRC LDNLFYVADV DTRNSTKCLF AEYLILAISI
MLASVIGFKF FAALQFGGKN LPEGLDKFVM CQIPAYTEDE ESLRRAIDSA ARMRYDDKRK
LLVVVCDGMI IGQGNDRPTP RIVLDILGVS ESVDPEPLSF ESLGEGLKQH NMGKIYSGLY
EVQGHIVPFL VIVKIGKPSE VSRPGNRGKR DSQMVLMRFL NRVHYNLPMS PMELEMYHQI
RNIIGVNPAF YEFMFQIDAD TVVAPDSATR MVASLINDTS IIAVCGETAL TNAKGSFITM
IQVYEYYISH NLAKAFESLF GSVTCLPGCF SMYRIRAAET NKPLFVSREV VEAYSTIRVD
TLHMKNLLHL GEDRFLTTLL LKFHSKYKTK YIFTAHAWTI APDSWAVFLS QRRRWINSTV
HNLIELMPMQ QLCGFCCFSM RFVVFIDLLS TIVAPVTVAY IVYLIVRVVQ HPSTVPITAF
ILLGAIYGLQ AIIFILRRKW EMVGWMIIYI LAIPVFSLGL PLYAFWHMDD FAWGNTRVVA
GEDGKKVLIS DEGKFDPESI PKKKWEEYQA ELWETQTSRD DTHSEISGFS YGTKAHGAMS
EYAYPSRPAS TTGFMQTAPH MQPYEARNMS RMSMAPSEMN RMSQYGGSQF FSPEDMVGLP
TDDQILSEIR DILKTADLMT VTKKGVKQEL ERRFDVPLDA KRAYINSATE ALLSGQL
//
