ID A0A178EJ66_9PLEO Unreviewed; 1198 AA.
AC A0A178EJ66;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=IQ07DRAFT_499673 {ECO:0000313|EMBL:OAL55844.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL55844.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL55844.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL55844.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441637; OAL55844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EJ66; -.
DR STRING; 765867.A0A178EJ66; -.
DR InParanoid; A0A178EJ66; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF16; CHITIN SYNTHASE 3; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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:UP000077535};
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 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1092..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1119..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 134666 MW; 0CF8D3723BD0066B CRC64;
MSLPQRPDES SPRRDQRHVF RDSPSRRRRT SDLENTRSTD RTTSKSGGQS YSRPLPSPGT
PVPMERDPVM RGQQSTTGPD LGRKRSLIRP ERQRIDPNHP NYHYRKHAQR MAVQPSTTGN
DPIMEDHMEA ETVSSDSTDL KPPHLRNASG GGYNDKQVPL EDGAPRVQRR LTRSKTMENL
EKQRQKEKDK MRPPSLWNVY CAIVTFWCPD AILKCFGKPQ KAQQRAWREK VGLVSIILLI
CTFVGYITFG FTETVCPAGG NARLRANKVD RGFLIVHGKA YDLARSTHPL ARGIPSGANV
LFDLPEKHGG QDASFLFQNV NGACKGLITP KAISSIPLGA NGDMAWYFPC RLFNQDGSTK
PNNTFVEYNG YMCHTSDNAR KAFYSLRNTG DVYFTWDDIR NSSRNLMVWG GDVLDLNLLD
WFNKTEVNTP PIFDEIRQNP SVRGVDVTRA YSSSYEKQVA RCFTETIKVG SIDTESIGCI
ASKVVLYVSL VFILAVVGAK FFLALAFQWF ISRKFGATKT SVGKADSKQR KQQIEEWSDD
IYRPPPRLAD PASGPDRSSK RGSTFLPSTS RFTSPYTMDK SAKTRAPPTT MTSQSNGSRL
LGSSNGGMYR QLNASHGTLP TYDGKHSTQE SRSSLLLSGT TEQARYSSVM GESEGPGPAG
FIHEAVVPQP PPEWQPFGYP LAHAICLVTA YSEGAEGLRT TLDSIATTDY PNSHKLILVI
CDGMIKGKGE DLSTPEICLG MMKDHAVLPH EVEAYSYVAV ASGSKRHNMA KIYSGFYNYG
EDSRIALDKQ QRVPMMVVVK TGTPDEAKKS KPGNRGKRDS QIILMSFLQK VMFDERMTEL
EFEMFNGIWK ITGISPDFYE IVLMVDADTK VFPDSITHMI SAMVKDPEIM GLCGETKIAN
KRQSWVSMIQ VFEYFISHHL AKSFESVFGG VTCLPGCFCM YRIKAPKGGQ NYWVPILANP
DVVEHYSENV VDTLHKKNLL LLGEDRYLST LMLKTFPKRK QVFVPQAVCK TTVPEEFKVL
LSQRRRWINS TVHNLMELVL VRDLCGTFCF SMQFVVFVEL IGTLVLPAAI AFTFYLIAIS
IKAAILHTTA PLIPLILLAL ILGLPAVLIV VTAHRWSYVA WMFVYLLSLP VWNFVLPTYA
FWKFDDFSWG DTRKTAGEKT KKAGLEYEGE FDSSKITMKR WHDFEAGKVH NRSRRYRH
//
