ID A0A074WPE7_9PEZI Unreviewed; 1767 AA.
AC A0A074WPE7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=M436DRAFT_62425 {ECO:0000313|EMBL:KEQ75010.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ75010.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ75010.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ75010.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584706; KEQ75010.1; -; Genomic_DNA.
DR RefSeq; XP_013429181.1; XM_013573727.1.
DR STRING; 1043004.A0A074WPE7; -.
DR GeneID; 25413370; -.
DR HOGENOM; CLU_000192_0_0_1; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000027730; 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; 1.20.120.720; 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; 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:UP000027730};
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 727..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1421..1445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1451..1474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1481..1504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1709..1765
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1767 AA; 196245 MW; 3C9D0F82705B77BD CRC64;
MAGPGSRLSV YSTHSNVPRP AQPSAQLSTT TLLNSLHSVW NNSQPYALES STSLVVNTWV
TSMMVGPDGR QGGTVDAELG RRAWEHARRR AEDGCVVLGS LHESTPSLLI PFLSSLPVAV
PASLYTALNA IRPFLHSVTP RNPSAAQHSG LAAVLNLNLE GELTGASLSL SSSGINVTKG
LTDVPAEIGY RAFDVFYYLL SSASPAEKEF LSLQEPKAYA LLKKTDTYTP PLYLPTADDA
AAADDFRASL KEIGIKGAAL RNMLSVVAAI LKLGETMGFL VDEDVLENVC EEVADLLDLD
TAVLTKKCDT MERQTLMAAI YEALVDWLIA RANEAIRMEV RNGGLVSSSN GSDTENSGGI
MTPPPGEEGA DTVNLTILEL PSATLGKAMA LRTVFDDSTG INLEMKEDGV PSYHVGSSIV
REMTDAVNDN AAELELTDSV AAREREEVLD RREALLEKVG VETEADSFLR RLLYPIEGEG
VQLGKTGRFS LMNLLGSSRV WFQLALHPTD ESPASLANHS PTSFPWSAGS VSSQIRSWRL
PEWANHRNKK LDYTADFDIN EFQERYARLG CQLGRDGVES WVMERGWSNG EVVIGHERIW
IREAPWWEAE SMLDLKPMDP SMDAAGPFGG QYQVSTPMVE DGFYQQPYHD NPSNPFLSRN
QSFASRSQLG AKSIAPSKAP TMQGRPGDYG LGPKGDDKHG EVTYYGDEED GDAKVIVEVP
ITFSRKVWVW AVWALTFYIP SPALRYIGRM KRSDVRQAWR EKFALMIIIF IINATVVFYI
VAFGRLLCPN MDKAWNAKEV SYHAASNDYY VSFRGHVYDL TKFHKIQHSD GVTQTTVANM
EPFGGTDVSE FIVPPISVAC YGLVGPDSTI SLTANDTTFT QEYPTAVHAS GPIAAPDKDS
ALNNINWYAD TFLPKMKEYY KGDLVVKTNK VRSDGQDNNH YWFTLGNKLY DMTDYFNTLN
LMNNLATYKF FPDEFSAIVQ SNAGQDIKSE FDKKITNVTE HSAITQCLDN MFYSGKLDFR
DSARCQVNNY ILLVFTIILC TVIVVKFLAA LQFGSKPRPA PQDKFVICQV PAYTEGEDHL
RKGLDSLTSL AYDNKRKLIC VICDGMIVGG GNDRPTPKIV LDILGVDPKI DPPALPFKSI
GSGAEQLNYG KVYSGLYEFE GNVVPYIVVV KCGKESEQVK AKPGNRGKRD SQILLMSFLN
RVHHRAPMSP LELEMFHQIN NVIGVDPELY EYLLMVDADT LVKEDALTRL VAACTNDSKI
AGICGETSLE NEEQSWTTMI QVYEYYISHH LSKAFESLFG SVTCLPGCFT MYRLRTADKG
KPLIIADAVI EEYSDCNVDT LHKKNLLSLG EDRWLTTLMT KNFPQMSFKF IPDAYAQTAA
PETWSILLSQ RRRWINSTIH NLAELMLIKD MCGFCCFSMR FVVFIDLFGT VILPATVVYL
VYLIITASTG GQFPLISIIM LAGVYGLQAI IFIAKRQWQH IGWMICYLAA YPLYSFVLPV
YSFWKQDDFS WGNTRVVIGE TGTKQVIATE IEEFDPRSIP LQRWDDYAFR NQLPGRRGLV
VQEKDGFSPF QDNGAYEMDD IRSVYSSVHP ASTILTGLPN NNMSYRPPTQ SPGPYNAYNR
MSSYSRFTDV MPGANENQRL MSMGNMSDAA PGLPRNYSGQ YLSSQPDLLS PKLSPPPSAG
FPPRSRSPLS QPTSRPASTF GLPGFQTQGV SDGQIVDAVR DCLREVDLDN VTKKQLKVLT
EQRLQVQLDP QKRAFLDQQI DFELANM
//
