ID A0A0F4GQJ1_9PEZI Unreviewed; 1729 AA.
AC A0A0F4GQJ1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=TI39_contig411g00027 {ECO:0000313|EMBL:KJX98450.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX98450.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX98450.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX98450.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) 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}.
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:KJX98450.1}.
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DR EMBL; LAFY01000403; KJX98450.1; -; Genomic_DNA.
DR STRING; 1047168.A0A0F4GQJ1; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000033647; 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; 1.20.120.720; 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; 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:UP000033647};
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 703..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1399..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1426..1447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1454..1477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1671..1727
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
SQ SEQUENCE 1729 AA; 192666 MW; 436131760AB72142 CRC64;
MQQVGTSQVS TTTLLNALHS SFSSGQPYQL ESSSSLVVNT WVTASSIGPD GRYGGTVDAE
LARRTWEHAR RRAEDGCVIL GSLHHSTPSL FAPFASALPL SIPGTFYTAL DALRPFLHTV
TPFNPSLPRY SALAGVFTLA LSGEITGASL SLSTAGIDTD AGLLNVPTES GYRAFDVFYY
LLTSQSEQER EFLGLKRPRE YALLRKSDTY DPPTYLPTAD DAAAAEDFRE SLKAIGIKGS
SLRSLLSVVA AILRLGDALG FLVNEEELAE VCEEVGGLLD LDPEVIFKKC STEDRDILIG
ALYEALVDWV IMKANEAIGS EIRTGRAIGS SNGSDNGAAT PLGSLEDGDS VSITVIEVTS
QTLGKAASLK TVFDDSNGIN AEMKEDGVPI VPAGSSVIRE MKEAVQRSEA DLDISGGNEA
REREMALDKR QEVLEKVGIE TEDESFLRHV LYPLDGQGVG LGRIGRFTLT DVMGCSRIWF
QLCLHPNEES PANFSNQSPQ NLPWSAGSVS SQIRAWRLPE WANYRSKQLD FTADFDVEEF
VERYRRLGCL DGKDGVESWI MERGWSNGEV VVGHERIWMR EPAYWEAESM LDMKPMDDMS
QINMLGGMDG GYPAGPGFDG PYYDDAITVH TRQPSHAAPS RMGAKSLAPT TAHTMRSASG
GDYGLGFKGD DKRNYVGFEG EIDGELTEGK EMLVQQTTTG RRAWVAVVWI LTWWIPSPLM
KLVGRMKRPD VRMAWREKVA LVMLIALLNA TIVFYIVGFG KILCPNRDKV WNLKQVGYHQ
GRTDYYVAFR GGVYDLTKFY KLQHSDMNNV PVTADDMLQF AGTDVSPYIV PPLSIACPGL
VDDQRLTLTP NETLPITNGE HISGPEVQND QNSALHSITW YSDKFLPKMR EYYKGKLVYK
RSAVKKDGED NSHMWFILNG EVYDLTDYFH SVDLFQGNDV YKFLPDDVTE LVQSNPGADL
TSKWVNSVPD YTNRTNTMNC LTNRFHIGST DFRDDARCQV NAYILLMFTV VLCTVIVIKF
LAALQLGSKK RPTQQDKFVI CQVPAYTEGE DSLRKGLDSL TALAYDNKRK LICVICDGMI
VGGGNDRPTP KIVLDILGVD PKIDPPALPF KSLGLGGEQL NYGKVYSGLY EFEGNVVPYI
VVVKVGKESE QTKSKPGNRG KRDSQILLMS FLNRVHHRSA MNPLELEMFH QINNIIGVDP
ELYEYLFMVD ADTKVKEDSL NRLVAACAND AKVAGICGET SLENEERSWT TMIQVYEYFI
SHHLAKAFES LFGSVTCLPG CFCMYRLRTA DKGRPLIISD KIVTEYADNN IDTLHKKNLL
SLGEDRYLTT LMIKHFPSMT YKFVPNAHAM TEAPSDWSVL LSQRRRWINS TIHNLAEMLT
VDLCGFCCFS MRFVVFIDLF GTIILPATFG YLVYLIINVA SGTGQFPLIS IIMIAAVYGL
QAIIFLVKRQ WQHIGWMIIY LLAYPIWSCI LPIYSFWKQD DFSWGNTRIV IGEKGDKKLV
AVDEEGYDPR NIPLQRWDDY ATANNLPGRR GYVQEKESIY QDGGYEMDDM HSVYSSVKPA
STILTGFPQH QSFRPPQSPG PFNAYGRQSA MSRYTDAPYQ AEQHQRLMSM GSNALFSPQD
FSQDNLLLRG GAHSPNNMMY DQQRTRSPMG TLAAHSRPGS MNQLSGFQTQ GVSNEAITVA
IRECLNEVDL DTVTKKQLKA LTEQKLQIQL PGDKRAFLDS QIDHELANM
//
