ID A0A167EFT4_9PEZI Unreviewed; 1800 AA.
AC A0A167EFT4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
DE Flags: Fragment;
GN ORFNames=CI238_11174 {ECO:0000313|EMBL:KZL85080.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL85080.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL85080.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL85080.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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:KZL85080.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFIW01000732; KZL85080.1; -; Genomic_DNA.
DR STRING; 1573173.A0A167EFT4; -.
DR Proteomes; UP000076584; 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; 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:UP000076584};
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 774..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 812..834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1079..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1458..1485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1491..1512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1519..1542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1742..1798
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1680..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL85080.1"
FT NON_TER 1800
FT /evidence="ECO:0000313|EMBL:KZL85080.1"
SQ SEQUENCE 1800 AA; 198956 MW; DB0D298FFD9906AF CRC64;
LLDDTNDPNS ASSLDVVVHA GHHDPNSIAM ANGRMSMYSV ASEGLGGPRA GQQPSQFSTT
TLLNAIHNIY LSSQPFKLDA GTSLVVNTWL TASQTGPDGR TGGTIDAALG ARAWEHARRR
AEDGCIVLGS LHTSSPSLLT PFLSSLPLSL PSSLYKSLEA IQPFLRCSTP YNPSTPRQSA
LGVTLTLNLA GNVHGAAIAL SQGGIDTAKG LLNVPAEAGY RAFDVFYYLL TSASTPAERE
FLGLKSASSY ALLAKSGTYD PPSYLPTADD AAAADDFRSA LKDIGIKGSA HRNLISTLAG
LLKLGDTLDY NLDEEVFDDI CEDVSGLLGM DPETLATQCT TEDRATLVSG LYEALVDWVI
AKANDAISAQ MARIRDGTES IGGGGARTPT SNGDGDTVCI TILDVPDPTL GKALAMRGVF
DDTLGINSEM IADGVEVPSA GSTVVREMQT AIGEVGPELG LMTGTIGKDR QHALEKREEV
LEKIGHSADE DAFLKKLLFP ITGQGINLGL TGRLDISTLL SSSRVWYHLS IHPTDDSPAS
LAALPSINSA WSAGTVSRQL RSWRLPEWAN RRNKNLDFTA DFDIDEFVQR YSALGCKDGR
EGIETWILER GWTNGEVVVG KERVWVRESA WWEAESMLDM KPLDNNLPGM GNVLAVNNLE
SGYSANGSGY FPTPMLDTTP NGSRDHLIAH QRNFSQGNLS QHTLAQNAAM RAPSIAPSGM
RNVQTGDYGL GTKGDTYKGQ VFYNNEGEFV GQMDPEIADG KHVEEKTMDK DRRIWVAIVW
FWTFWIPSPL LRFVGRMKRP DVRMAWREKL TLVWFIVLIN AAIVFWIIAF GRILCPNFDK
AWNAEEVSQH GGETDFYVSF RGGVYDISKF WKTQHSDTAI ETTKENMIQF AGLNMDDYFP
PPLPLVCPGL GIATTTTLQY NTTPEYTIGI HKSGSLADDR TSALGATDWY SKKLLPRMKE
FYKGDLVWDK GDIKSDGQDN SHMWVIYEGG VYDLTNYFKT LDVFKRVDSV KFLNTKIVSA
IENNPGEDIT DNWNEIIKSA ASNSTENASV QNSLNCIKNL FYVGIPDFRY SARCQTNNYI
MLAMTVILCS VILIKFLAAL QFGSKRRPAP QDKFVICQVP AYTEGEDSLR KALDSLTALQ
YDNKRKLICV ICDGIIVGAG NDRPTPKIVL DILGVDPKVD PPALPFKSVG TGSEQLNYGK
VYSGLYEFEG NVVPYLVVVK CGKESEQSKS KPGNRGKRDS QILLMSFLNR VHHRAPMSPL
ELEMFHQINN IIGVDPELYE YLMMVDADTC VREDSLNRLV SACANDAKIA GICGETGLQN
DDKSWWTMIQ VYEYFISHNL AKAFDFTMYR LRTVDKGKPL IIADGVIRDY AVCDVDTLHK
KNLLSLGEDR YLTTLMTKYF PSMKYKFIPD AYCQTAAPES WSVLLSQRRR WINSTIHNLF
ELMKLKEMCG FCCFSMRFVV FIDLFGTIIL PATTIYLGYM IYLAASGTGQ FPIISIIMLA
AVYGLQALIF ILKRQWQHIG WMIIYILAFP IYSFALPIYS FWNQDNFSWG NTRIVIGEKG
NKQIVAVDDE GFDPRSIPLQ RWDDYAMANN LPGRRGGYME KADMGYDDQY EMDEIRSVYS
SVRQGSVLTG MNRNNTYMPP QSPAPFGHMA RASGAASPYH HDQTMANRQS MASLGTHDIN
RGQTPFQDFP SSRPSVTNLR GQANLSPGLG ANRSQSALGL NRPHGAAQST SSFDFQRGNM
QGPDDGMIIE AIQGVLREVD LDTVTKKQVR ALVEQRLQTG LVGERRTFMD RQIDNELANM
//
