ID M5BVM2_THACB Unreviewed; 1915 AA.
AC M5BVM2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 28-JUN-2023, entry version 56.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=BN14_04605 {ECO:0000313|EMBL:CCO30575.1}, RSOLAG1IB_09005
GN {ECO:0000313|EMBL:CEL59007.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO30575.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO30575.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Isolate 7/3/14 {ECO:0000313|EMBL:CCO30575.1};
RA Jelonek L.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCO30575.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065},
RC and Isolate 7/3/14 {ECO:0000313|EMBL:CCO30575.1};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
RN [3] {ECO:0000313|EMBL:CEL59007.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL59007.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) 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; CAOJ01006652; CCO30575.1; -; Genomic_DNA.
DR EMBL; LN679136; CEL59007.1; -; Genomic_DNA.
DR SMR; M5BVM2; -.
DR STRING; 1108050.M5BVM2; -.
DR HOGENOM; CLU_000192_0_2_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR Proteomes; UP000059188; 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; 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 Glycosyltransferase {ECO:0000313|EMBL:CCO30575.1};
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:UP000059188};
KW Transferase {ECO:0000313|EMBL:CCO30575.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 935..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1231..1253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1630..1651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1657..1678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1685..1708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..797
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 998..1060
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1854..1909
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 602..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..685
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 869..888
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 1915 AA; 214696 MW; 2F8AFC47817DAD5D CRC64;
MSGGLTHQQK LESVDDLSAL YPSISDDIIV SCLRERFLSD TIYTAVGSHA LVALNPHKYV
NASADSVLMQ YASEYRDAER DGPPREPHIF QLANNAYYHM RRTTQDQSVV FFGETASGKS
ENRRLAIKSI LELSVPNPGK KGSKLSQQIP AAEFVLESFG NARTLFNPNA SRFGKYTELQ
FNDRGRICGI KTLDYYLERN RVAGAPNGER NFHIFYYLTA GAGPEERQHL ALTDKTTFRY
LGAGQRPMAG MQPKPGMSGG SNEDWARFEQ FKMAMKHVGM SKRHIAQSCQ LVAAILHLGN
LEFTRDRSRN EDAAVVRNVD VLELTAEFLG LQASALESVL SYRTKLVKKE LCTVFLDEDG
AADNRDDLAK TLYSLLFAWI NETINQRLCR EDFSTFIALF DLPGTQNLPP SASRSNSLDQ
FCVNFANERL HRWIQQSIFE AHTEEYTTEG LAARWSPSIP YFDNSECVRV MGNKPGGLIH
IMDDQARRMP RKTNQTMVEA FGKRWGNHSS FKVGAADRSG LPTFTISHFN GPVTYSSENF
LERNSDALNP DFVSLLRGST SEVLGGGEPS TDGSRNPFIK GLFNGRAIAT QAHPRNEDTI
VAAQQPQKPM RAPSTRRKGT VSRRNRMPTL GEEGENGDEA AAAAEDSAPS GIKCIAGEFR
SALETLFETL DDTQQWFVFC INPNDGQLPN QLEGRGVKAQ VRSIGLPEIA RKSGVVWEAN
MTDEEFLERY KETVVKADVS EGEGGMDEAD RIGRVRVMLG LSEGDIVIGK ERVFLSHAAF
HKLENPLRAQ DLEEQKRNKL REMEAEAGFE PRVADPYAPY PSPGMEPNSP YYGGGNAYDQ
SSQHIPLVSH AQSTPLMAPQ AGFMYDDDKS MGGSDGRGGD DAMSMSVGSE SYAPSRQLFT
AADRQPVPDK EALPGEVMSG ETTEEVKTTA ARRRWVAFCW MITFWIPNFI LAHIGRIKRV
DVRQAWREKL AINMIIWFIC ACAIFVIAVL GTLICPTDHV FSQNELQSHS NTNDPNNVYT
SIRGEVFDLS NLVIAHTVQV KVVPSKSILN YGGDDASDLF PVQVSALCNG ITGTVSPWVI
LDTTNQTMNV NAQYHDFRAF TNDPRADWYY ESMVRMRYMY RKGFMGYQPK EISNMAKNRR
AVGIIDGMVY EMTNFAPGIR APEGEQAPAG IDRNFMSQEI ISMFMQNSGS DMSKLINQLG
LDADVLARQR TCLRNLFLIG KVDHRNSPQC LFATNILLAL SVVMVSIIGF KFIGALHFGT
PRAPEDHDRF VICQVPCYTE GEDSLRRTID SLAKLRYDDK RKLLFVVCDG MIVGSGNDRP
TPRIALDLLG ADPNIDPEPL SFLSLGEGAK QHNMGKVWSG LYECEGHVVP YIVVAKVGKP
TERSRPGNRG KRDSQMVLMH FLNKVHFNSP MNPLELELYH QIKNVIGVNP TFYEYVLMVD
ADTTVEPLSL NRLVSAMIHD KKVLGVCGET SITNAKQSII TMMQVYEYFI SHHLSKAFES
LFGSVTCLPG CFTMYRLRSP DTHKPLFIAQ QIIDDYSENR VDTLHMKNLL HLGEDRYLTT
LLLKHFSNYK TQFVRDAHAY TVVPDEWSVL LSQRRRWINS TIHNLGELVF LDRLCGFCCF
SMRFIVFIDL LSTVTQPVTV VYIVYLVYLV VGEGKPVPTL ALIMLAVIYG LQALVFIFRR
KWDMIGWMIF YILAIPAFSF LLPLYSFWKM DDFSWGSTRL VVGEGNKKMI VHDEGKFDPR
SIPLKTWTDY ENELWDKESN HSIGSWVPPS KKEIPWDAQT QSMYGRETLF EQPMSRAYSP
APSQGGMYMP AHHGNSGSGG RGTPIGGRQY PQTTMSRPAT NYLDMPAHMF SGDGPSDAEI
EKAIQDILSA ADMSQVTKRT VRTQLENGFG INLTSRKDFI NSVIEREVAA RMPQD
//
