GenomeNet

Database: UniProt
Entry: K1VBY9_TRIAC
LinkDB: K1VBY9_TRIAC
Original site: K1VBY9_TRIAC 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system