ID A0A225AGG3_9EURO Unreviewed; 1763 AA.
AC A0A225AGG3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=UA08_06696 {ECO:0000313|EMBL:OKL58253.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL58253.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL58253.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL58253.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:OKL58253.1}.
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DR EMBL; LFMY01000010; OKL58253.1; -; Genomic_DNA.
DR RefSeq; XP_020118374.1; XM_020269002.1.
DR STRING; 1441469.A0A225AGG3; -.
DR GeneID; 31006451; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000214365; 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 CDD; cd04190; Chitin_synth_C; 1.
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 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; 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; 2.
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:UP000214365};
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 729..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1423..1444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1450..1471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1478..1501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1705..1761
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
SQ SEQUENCE 1763 AA; 195934 MW; 89C0BB594D77D44A CRC64;
MSHRYSMFST TSAPGLPKSS SQISTTTLLN SLHNIYSSAQ PYPLEVGTSL VVNTWLTVAN
LKPDGTPGGT VDVELAVRAW EHARRRAEDG CIVLSALHRS CPIILPSFLS ALPLSTPEVL
FTAFDAIRPF VSAVTPFNPS YSLYSSLAVS YTFTLGGSIT GVKLALSKSG LNLTRGLLDV
PSEPGYRAFD VFYYLINAAS SQAEREYLSL NDCSAYSILN KSGTYDPPSF LPTADDAAAA
EDFRSALKAI GIRGSSQRGL LSVLAGLLKL GNTLGFLVDE EDLEQVCEEA AELLGVDPDI
LLRGCSTDDR TILVTGIYEA LVDWVISKAN EAIATQIRAD QENGSSDGSG APWHTEDVSD
TVTITVIDIP SPPLGKAVAL QGVFNDNQGI NAEMKEDGVE INSPGQSVLN EMHNAVSEVE
AELGIAESVA FREREHLNDR RQTVLEKVGI EVEMGGFLRE ILFPNENEGI NVGTRGRFDL
ASTLGSSRVW YHLSLHPTDD YPETLAQNTS AWSAGAVSRQ LRDWRLPEWA NRRHKQLDFT
ADFDVDEFVT RYSPLGCKEG KDGVESWILE RGWSNGDVIV GHERIWMREN AWWDAESMLD
LKPHSHSPVL PANPFESGYS ATPPNPNGSG FFPPMPMADN GSFIGSSEHL VNINRQGAMS
PGVARSLAPT NTHTLHNIGG DYGLGPKGDD HRGDDAYYAA ELSRLAGDDP EIAQRKHIEK
KKITLGRRLW AAFVWAATFW IPSFLLRYVG RMKRPDVRMA WREKLVLVTL IVLFNALMVF
WIIAFGNLLC PNKDKVYNEK QLSENQGDND FYVGVRGVVY DISKFWRLQH SDTSITTSAS
NMQWAAGQIL DAYFPVPLTQ GCPAFVTSDR IYLQNNNTDA VAESEALHNS GPYLQSDTTS
ALYNITWYAD TFLPFIHQYY KGPLVWSKDT ITQQANDDSR YWVIINNGVY DLTNYFYTAT
LFDDNSDYDF LPSAVTTLVK DNMGSDITSK WQNSTSFQNA LTCMKNVFYV GEVDFRGSAR
CTVNNWILLA FTILVCAVIL VKFLAALQFG SKPRPVPQDR FVICQVPAYT EGEDALRKGL
DSLTALQYDN KRKLICVICD GMIVGGGNDR PTPKIVLDVL GVDPKVDPPA LPFKSIGEGS
DQLNYGKVYS GLYEFEGNVV PYIVIVKVGK ESEQSKSKPG NRGKRDSQIL LLNFLNRVHY
RAPMSPLELE IFHQINNVIG VDPELYEFLL MVDADTSVKE DSLNRLVAAC VNDARIAGIC
GETSLQNEEG SWWTMIQVYE YYISHHLAKA FESLFGSVTC LPGCFCMYRL RTADKGRPLI
ISDNVIQEYS EGDLDTLHKK NLLSLGEDRF LTTLMSKHFP TMFYKFIPDA FASTAAPETW
SVLLSQRRRW INSTVHNLVE VAALKDLCGF CCFGMRFIVM IDLMGTLILP ATCVYLVYLI
YLVASHKGTF GVISIVLLAA VYGLQAVLFL LKRQWQHIGW MLIYLCAYPI YSVILPMYSF
WKQDDFTWGN TRVVIGEKGD QRVVAVEDEV FDPRSIPLQR WDDYALANNL PGRRGNFDYS
EEKRYLPPYA DETAMEMDDF RSTYSSVKPA STVLTGFPGG RGPYMPPQSP APFAGNNRNS
RMSSFTRYTD APQLGGHAQR HMSMGNISTS YQDNPVNASR LSMPMMQSSE NLLGVPNRQR
SPLGGAYGPR PVSTVMDFRS GPGHGPDDAT IVDAIRQVLA EVDLDNVTKK QVRALVEQRL
QTELAGERRT FVDTQIDQEL ANM
//
