UniProt: G4TNQ7

Database: UniProt
Entry: G4TNQ7_SERID

LinkDB:  G4TNQ7_SERID 
Original site:  G4TNQ7_SERID

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   G4TNQ7_SERID            Unreviewed;      1907 AA.
AC   G4TNQ7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   28-JUN-2023, entry version 65.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=PIIN_06905 {ECO:0000313|EMBL:CCA72950.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA72950.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA72950.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA72950.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
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:CCA72950.1}.
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DR   EMBL; CAFZ01000192; CCA72950.1; -; Genomic_DNA.
DR   STRING; 1109443.G4TNQ7; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   HOGENOM; CLU_000192_0_2_1; -.
DR   InParanoid; G4TNQ7; -.
DR   OMA; LEMHHQI; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000007148; 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; cd04190; Chitin_synth_C; 1.
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; 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.
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:UP000007148};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        907..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        947..966
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1214..1236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1607..1625
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1632..1651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1657..1678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..762
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1849..1904
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          582..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..656
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1789..1819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         105..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1907 AA;  214752 MW;  A55968C441A9E764 CRC64;
     MSKFEGIVDL SKLQNINEDV LGAALRDRFL SDTIYTAIGS SAIVAVNPHK YVTCNSDAVL
     AGYAHEYRDT APSKVQNPPH IFQLANNAYY NMRRTSQDQS ILFTGETGSG KSENRRLALK
     SIIELSSSNP GKKGAKLASQ IPSAEFVLES FGNARTMYNP NASRFGKYTE LQFSERGRLS
     GVKTLDYYLE KNRVAGVPSG ERNFHIFYYL LAGASQEERQ HLHLVDKATY KYLGPYRRPL
     DRDDDANRFE QLKIALKTIG FSKRHVAQTC QLLAAILHLG NLDFTVDKHR NEDAAVVRNT
     DILEIVAEFL GVPPGDLEAV LSYKTKLVKK ELCTVFLDEE GAAMNRDDLA KTLYSLLFAW
     LNESINQKLC RDDFATFIGL FDLPGSQNLP QGAIRTNSLD QFCVNFANER LHNWIQKRIF
     DRHTEEYAAE GIQQFSPQIQ YFDNSECVRM ITHHTGGLIH IMDDQARRAP KKTEHTMLEA
     FGKRWANHSS FKAGGTDRTG FPTFTINHYN GAVTYSSESW LDKNHDALNP DFVSLLRGSN
     IAAASEQQGS NNPFIQGLFS AQAIATEAHP RNQETIVAAK QPVKPMRAPS TKRKQTIRRA
     GTQKRKGDGA IAEEEDEDAP NEIKCVAGEF NTSLTLLLET LDETESWFVF CINPNDSRLP
     NQMENRGVKA QIRSMGLSEV AKKNAVVLEV NMSFAEFRDR YGDVLRQANA SGLTDNPTAA
     EAAQIASAMG LGSKDIIVFL THKAFHRFED PLRASDVEEQ KRNRMRDAEA EAGMTMTGDT
     FSPYQTGPPS GEPTPYTAGP YGDPFGQSGS QAALPLVAHA QPFQRADMYE YDDHKSLRSD
     DFDAQSRFTS QRDDVGSNFG TESYAPSRNM FQNADRRVAA NKDPLPGEIM EGEVSEEIKD
     TPARRKWVAL CWALTWWLPN FVLRWVGRMN RMDVRQAWRE KLAINMIIWF ICGCAVFVIA
     VMGNLICPRE YVFDSGEVSD HSYLHNPKAT YISIRGEVFD LTKIAQAHFR TVPVVPQKLV
     LKYGGTDASE LFPVQVSALC QGKTGSVNPY VTLNSVNTTD DANNIYHDFR AYRSTGDGDW
     YNYRPDWYFE QMVVMRYHYR LGFVGISPSD VRNRANNGRL IAIYRGLVYD LTDYVNAPPS
     IKVPDGQAEP GGIDRFFMHD AIVDVFKQQA GKDVTKLIDG LSIDPQVLQW QRTCMRNLFT
     IGKADRRQSV QCQFATYILL VLSCIMVSII GFKFLAALHF GSPRAPEDHD KFVICQVPCY
     TEGEDSLRRT IDSLAKLKYD DKRKLLFIIC DGMIVGSGND RPTPRIVLDI LGADPNLDPE
     PLSFHSLGEG AKQHNMGKVY SGLYECAGHV VPYLVLVKIG KPTERQRPGN RGKRDSQMAL
     MHFLNKAKLE MYHQIKNVIG VNPTFYEYCF MVDADTVVDP LSLNRLVSAM MHDKKVLGVC
     GETSLANSKQ SIITMMQVYE YFISHHLAKA FESLFGSVTC LPGCFTMYRL RTADTHKPLF
     ISKQVIEDYS ENRVDTLHMK NLLHLGEDRY LTTLLLKHFP NYKTQFVRDA HAYTVAPDEW
     SVLLSQRRRW INSTIHNLAE LVFLDRLCGF CCFSMRFVVF IDLLSTLVQP VSVAYLGYLV
     YLVAVEHKMI PQLSLIMLAA IYGFQALIFI FRRKWDMIGW MIFYILAIPA FSFFLPLYSF
     WKMDDFSWGA TRVVLGEKGK KLIVHDEGKF DPRSIPLKSW NDYENELWDK ESNHSIGSWI
     PPEREFGHAE SRGQSLYGGT QYDMPRSRSF SPAPSLGLNS AFAPLAYPAG SGGNTPGDPH
     GSRPASRTML HGSASRPPTA YLDMPMPRAA SPMMGGFDYD QAAASPTQGP SDHELENAVR
     ELLRNADLNS VTKRAVRQKL EERFGMDLSA RKTTINSTID RVLLSQN
//

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