ID A7TJZ0_VANPO Unreviewed; 1173 AA.
AC A7TJZ0;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=Kpol_1037p49 {ECO:0000313|EMBL:EDO17452.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO17452.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480404; EDO17452.1; -; Genomic_DNA.
DR RefSeq; XP_001645310.1; XM_001645260.1.
DR AlphaFoldDB; A7TJZ0; -.
DR STRING; 436907.A7TJZ0; -.
DR GeneID; 5545672; -.
DR KEGG; vpo:Kpol_1037p49; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_002572_1_0_1; -.
DR InParanoid; A7TJZ0; -.
DR OMA; SLWNVYC; -.
DR OrthoDB; 1331060at2759; -.
DR PhylomeDB; A7TJZ0; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
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 SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1037..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1065..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1091..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 375..453
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|SMART:SM01117"
FT REGION 20..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 132702 MW; 36F6DAFB42D9B89E CRC64;
MMKGHSDDYY VQFDQDNEGL LNSNRGSLRS NSRINRQNSL IRPERNRLNN PDNPHYYYVQ
KTKEQRGKIA VQPSSTGLDP NLLPNNDDAE LRSGGGFNIH KNNSIRSRRT GHESLGKESD
IRESIELDDL DLAGLQNDPF MKSSIQIDES TNMLYETNPN AKNAKPNSND KEKESLSLWQ
LYCYIITFWA PAPLLSLFGM PKKERQMAWR EKIALISIIF YLGAFVAYIT FGFSRTVCKD
PPIRFKNNQV STSYLIINGK AYNLDSSSHP AAAGIEAGTN VLYPPIGYGG MDASFLFQNV
NGNCLGIINP RDNATTPFDD NGNMAWYFPC KPFSQDGSTK PNFTESEYYP GWACHTSEES
RNAYYSLNSN ADVYFTWDDI KNSTRNLVVY NGHVLDLSLL DWLETDQLTY PALFDDLRKS
NLQGYDLSIV FTTSHEKKIG RCLTEIIRVG EVDSKTVGCI VSDIVLYVSI VFILSVVVAK
FIVACYFRWI VSRKQGAYVI DNKSMVKHIN EIEDWSENIN SQGLNIGSQK PTFPGDQFPS
NASRMETHKR RGSKFLPLNE VTLDLNNDSM RFGKSGDVVT MSTQNALRVS NETPDNKSFY
GLHSRNPSAL ISSTSLLWNG AATNPMAAAS EVRSLDPTDI HPDVVQQPPV DYMPFDFPLI
HTICCVTCYS EGEQGIRSTL DSLTTTDYPN SHKLLMVLCD GLIKGSGNDK TTPETVLEMM
TDFVIPPDEV QAYSYVAVAS GTKRHNMAKI YAGFYKYDDE TVPSERQQHV PMIVVVKCGT
PDEQGSAKPG NRGKRDSQII LMSFLQKITF DERMSELEFQ MLKNIWRITG LMADFYETVL
MVDADTKVYP DSLTHMVAEM VRDPMIMGLC GETKIANKRQ SWVTAIQVFE YYISHHQSKA
FESVFGSVTC LPGCFSIYRI KSPKGSDGYW VPILANPDIV ERYSDNVTTT LHKKNLLLLG
EDRYLSSLML KTFPKRKQVF VPKAACKTIA PDSFKVLLSQ RRRWINSTVH NLFELVLIRD
LCGTFCFSMQ FVIGMELLGT LVLPLALCFT IYVIVFAIIS NPTPILTLVL LSIILGLPGL
IVVVTATRWS YLIWMLIYLF ALPVWNFILP SYAYWKFDDF SWGETRTIAG GNDAEGKDDI
EGEFDHSKIK MRTWREFERE NLRNSQTIEP ALY
//
