ID K1VBY9_TRIAC Unreviewed; 1942 AA.
AC K1VBY9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=A1Q2_07344 {ECO:0000313|EMBL:EKC98330.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98330.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98330.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98330.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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:EKC98330.1}.
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DR EMBL; AMBO01000391; EKC98330.1; -; Genomic_DNA.
DR STRING; 1220162.K1VBY9; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_2_1; -.
DR InParanoid; K1VBY9; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14879; MYSc_Myo17; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 3.40.850.10; Kinesin motor 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; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036037; MYSc_Myo17.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
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; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Transferase {ECO:0000313|EMBL:EKC98330.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1224..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1616..1643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1649..1670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1677..1700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..771
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 975..1037
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1886..1941
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 594..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..670
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 781..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1785..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1942 AA; 218249 MW; 540AC12E51449C63 CRC64;
MSSLRPTGGG QNKRFSTRFE GISDLCALPS IAEDTIIASL RERYVTSQPY TAVSDSALVS
MNPLTALPVN SDASLHDYVK EYFQSAGDDI VGQPGGKESL GPHIFRTTLN AYYNMRRTGQ
DQIILMSGAT GSGKSEMRRL AIKAVSEVSV APHGKKGYKF ILESFGNAHT VHNDNASRYG
NYTELQFTDR GRLEGLKTIE YYLERSRVSQ VPASGERNFH VFYYLCAGID GEERQHLRLG
NEGDYHYLQS RARRTGASDR ERFRQLKQAF RAVGMSNRLV AQVCQLLACI LHIGNLQFSG
DDALHEGALV LNEDVLSTVA EFLGVHENAL AEIFSFKTLL VRKEVCTTFL DVEGAESVRD
ELARTLYSLL FSWLNEHLNQ KLCKDSFGSF IAILDLPGQQ NNAGPTLGIN SIDQFCFNFA
AEKQHNWILH RIHEAPLAEA AADKMPLDRI PYFDNTECLK MLSDPKTGLI AIADDQSKKK
RTDNQMLDAM AKRYTGHSSF AVGNMDRTGS ASFTVNHYGG PVTYSVEGFT DRNANETSAD
ILRLLRGSAT GPTHVPDAQG SNNPFIRTLF SSRSIATQMH PRNEDTIVAA QQPVKPMRAP
STRRKRAGSR LRAVQETEGE DAEVGGGNDE GNAGTQLHCV AGQLWQALSG LFATFDQIQP
WFVFCLRPND SQLPAQVETR SVKAQIRSLG LTEISQRLRS ADFEVRMTHQ EFADRYYDEF
AERAIGNQGT TADRIRDLKR VLQLDDHHML VGSSRVFLSH ATFHRFEDRL RESDGLEMPE
HLAAGPADKD DHFAPGHRTH SPEPEPMFDF HQERNFARND STAALPLVAN AAPAPQYPSS
EPDDESRGFA PSQATSAFGD SQSVAGTDAY APSRNMFHDM EKTRGEKDVL DELPEDNEVQ
EEYKESPARR RWVLLCRLLT WWIPDFALSR LGRMKRQDIR QAWREKLAIN LIIWFICGCT
IFVIAGLAPV ICPTQHVFTQ AELNSHNYKE NPKSAYTAIR GEVFDFTSFL GTHQRIVPIV
DSKTMQPYSG VDASSLFPVQ VSAVCSGTNP NGISPYITLD ATNQTNPFSQ YHDFRASHTS
TDFRPDWYRE QMMTLGGGYR KGWMGFTKKD LKHKADNKEV VGIIDGYIYD LTTYYNQGGG
GIQFPKDLDE TSEAATSAYA QRAFMADQVT QMFLQNSGKD VSKLWHDNVR KALGDEVWNM
QSDCLRWLFI VGKLDTRDSP QCLFSTYILL ALSCVMVAII AFKFLAAIHF GPSRAPENHD
KFVICQVPCY TEGEESLRRT IDSLVKLRYD DKRKLIFVIC DGNIKGFGNE KPTPAIVCDI
LGVDPNLDPE PLSFLSLGEG SKQHNMGKVY SGLYECAGHV CPYLIVVKVG KPSERPKPGN
RGKRDSQMLL MHFLNKVHFN SPMNPLELEI YHQIKNVIGV NPSFYEYLFM VDADTTVDEL
SLNRLVSACM HDKKIVGICG ETSISNAKQS IVTMSQVYEY FISHHLAKAF ENLFGSITCL
PGCFTMYRLR TPDTRKPLFI SNQIIHDYSE NRVDTLHLKN LLHLGEDRYL TTLVLKHFPT
YKTKFVRDAR AQTVVPDDGK VLMSQRRRWI NSTVHNMAEL IFQDNMCGFC CFSMRFVVLI
DLISTIIAPV TVGYIVYLIY IIVKSGSNIP ILSIAMLAAV YGLQALVFIF RMRWDMVAWM
VFYILAIPFF SLYLPLYSFW RMDDFSWGST RLVVGEKGKK VVIHDEGKFD PKQIPLKSWN
DYENELWDQE SNHSLDTWAA PQKSDYMGDG GSIYGAPSMY NQSQYGGQSQ YGGQSQYGQS
QTGRGSVYPP SSFYSHGPTA SQENLRAGSR NESYYERAPR GTFYDREGDT GSFHPGDNNS
MYASSFYGQP PLQPVNSNYG LPQDDGPTDM QLEASIRRIC QGADLDTLTK KGVRKQLESE
YGRNLASRKD TINKIIEDVL AE
//