ID A0A0K6G026_9AGAM Unreviewed; 1914 AA.
AC A0A0K6G026;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 28-JUN-2023, entry version 35.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=RSOLAG22IIIB_04811 {ECO:0000313|EMBL:CUA71865.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA71865.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA71865.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA71865.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CYGV01001267; CUA71865.1; -; Genomic_DNA.
DR Proteomes; UP000044841; 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; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; 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; 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:UP000044841};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 934..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1230..1253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1656..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1684..1707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..798
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1853..1908
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 602..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..686
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1793..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1914 AA; 214425 MW; D1872ED7115257D9 CRC64;
MSGGLTHQQK LESVDDLSAL YPSISDDIIV SCLRERFLSD TIYTAVGSHA LVALNPHKYV
NASSDPVLMQ YASEYRDAER DGPAREPHIF QLANNAYYHM RRTTQDQSIV FFGETASGKS
ENRRLAIKSL LELSVPNPGK KGSKLSQQIP AAEFVLESFG NARTLFNPNA SRFGKYTELQ
FNDRGRICGI KTLDYYLERN RVAGAPNGER NFHIFYYLTA GAGPEERQHL ALTDKTTFRY
LGAGQRPMAG MQPKPGMSAG GNEDWARFEQ FKMAMKHVGM SKRHIAQSCQ LVAAILHLGN
LEFTRDRSRN EDAAVVRNTD VLELTAEFLG LQPSALESVL SYRTKLVKKE LCTVFLDEDG
AADNRDDLAK TLYSLLFAWV NETINQRLCK DDFSSFIALF DLPGTQNLPP SASRSNSLDQ
FCINFANERL HRWIQQSIFE AHTAEYTAEG LAARWSPSIP YFDNSECVRV MSTKPGGLIH
IMDDQARRMP RKTNQTMVEA FGKRWGNHSS FKVGAADRSG LPTFTVNHFN GPVTYSSDNF
LERNSDALNP DFVSLLRGSA SEVLGGGEPS ADGSRNPFIK GLFNGRAIAT QAHPRNEDTI
VAAQQPQKPM RAPSTRRKGT VSRRNKMPTL GEEGEGGEEP ATGAAEDTSP SGIKCIAGEF
RSALDTLFET LDDTQQWFVF CINPNDGQLP NQLEGRGVKA QVRSMGLPEI ARKSGVVWEA
NMTAEEFLER YKDTVVKADV SEDEGGMSEV DRIGRVRTML GLTEGDIVIG REKVFLSHAA
FHKLENPLRA QDLEEQKRNK MREMEAEAGF EPRAADPYAP YPSPGMEPQS PYYGGNAYDQ
SSQHIPLVSH AQSTPLMAPQ ASFMYDDDKS MRSDERGGDD AMSMSIGSES YAPSRQLFTA
ADRQPVPDKE ALPGEVMNGE TTEEIKVTAA RKRWVALCWM LTFWIPNFML SHVGRIKRMD
VRQAWREKFA INMIIWFICG CAVFVIAVLG VLICPTEHVF SSNELASHST TNDPNNVYAS
VRGEVFDLTQ LSIAHGIRVS VVPSKSILSY GGTDATKLFP VQVSALCNGI TGSVSPWVVL
DTTNQTSNVD AQYHDFRAFT NDPRADWYYE SMVRMRYMYR KGFIGYQPKE IKNMAQNRRA
VVIIDGLVYE MTNFAPGRRA PEGQQAPANV DVNFMHQSII SLFNQNSGSD VSKLINQLGL
DADVLARQRT CLRNLFLIGK VDHRNSPQCL FATNILLALS IVMVSIIGFK FIAALHFGSP
RAPEDHDRFV ICQVPCYTEG EDSLRRTIDS LAKLRYDDKR KLLFVICDGM IVGSGNDRPT
PRIALDLLGA DPNLDPEPLS FLSLGEGAKQ HNMGKVWSGL YECEGHVVPY IVVAKVGKPT
ERSRPGNRGK RDSQMILMHF LNKVHFNSPM NPLELELFHQ IKNVIGVNPT FYEYVLMVDA
DTTVEPLSLN RLVSAMIHDK KLLGVCGETS ISNAKQSIIT MMQVYEYFIS HHLAKAFESL
FGSVTCLPGC FTMYRLRSPD THKPLFIAQP IIDDYSENRV DTLHMKNLLH LGEDRYLTTL
LLKHFSNYKT QFVRDAHAHT VVPDEWSVLL SQRRRWINST IHNLAELVFL DRLCGFCCFS
MRFIVFMDLF STITQPVTVA YIIYLVYLVA GEGKPLPTLA LIMLGVIYGL QALVFIFRRK
WDMIGWMIFY ILAIPAFSFL LPLYSFWKMD DFSWGSTRLV VGEGNKKMIV HDEGKFDPRS
IPLKTWTDYE NELWDKESNH SIGSWVPPSK KEIPWDAQTQ SMYGRETLYD QPASRAYSPA
PSQGGMYMPA HHGNSGSGGR GTPVGGRQYA QTTMSRPATN YLDMPAHMFS GDGPSDAEIE
RAIQEILASA DMSQVTKRTV RTQLESAFGV NLTSRKDFIN SVIEREVAAR MSQD
//
