ID A0A0L0V8C5_9BASI Unreviewed; 1567 AA.
AC A0A0L0V8C5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PSTG_11132 {ECO:0000313|EMBL:KNE95527.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE95527.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KNE95527.1}.
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DR EMBL; AJIL01000095; KNE95527.1; -; Genomic_DNA.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000054564; 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:InterPro.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR CDD; cd04190; Chitin_synth_C; 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 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; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF13; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR SMART; SM01117; Cyt-b5; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 429..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1116..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1177..1200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..258
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1508..1564
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 143..165
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 272..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1567 AA; 173121 MW; 63CB97C890D637BB CRC64;
MHSHFASHPS FISRPSHSTS QSVFGIKHWS GPVSYDASGI IQADLGLVDV EFVTLLRNSS
DSFVSRLLSG PSLALDRHPL DPSVLVAAQV SSSPLRRPSP ILPTHPHISL EPGSPRGAPL
DSTVALIDTS VVQPTLSQLN ATLSQFISHF SQCQVWNVLN IKPNEELYAN DWDPVRVRHQ
LNALRVPELI VRKKVDYPFD FDLTMFSMRF RLEGTEANDL RRQLSTGLML EENQDFAIGR
SRVWLTFRAF QSLEERLSAE QPAGSQQRPI AGHLAGFDIP GGSPRELDSW GDLGGGGSGS
YQHLIPSGSG NGDDRPNSGY EAERNIPQSP GFGGEGQLHD APHGGPMGYH DGPAQSRVWG
SEWESKQPME EQDMLSKEER YMDVGMIKHN QVGGQIEGNT NRDGATDAVL LKTDQNQTLE
EVESSKARMW WVVIVWALTF YIPNFLLSTI GRMKRPDIQM AWREKVALCL IIFLMCGSVL
FVILGLGKIT CPNLAKAWTP NELGFHATES DFYVGVRGQV FDLAKFWRGQ HSDITGQPVT
NSDMLSLAGQ DLTNYFPVPL KLACPNVLVD TVNLQFENWT ATVPNAVHVS GSGQVVKASA
LGNEKWYTEK FLPFMTNFYK GPIVYTRKLI AGLADNRAVG IYNGGVYDLS DYFYTYNTQN
RNPQFQYIDK SITDLFQQQP GKDITKEING LPMSDADKSA SLTCLRNLFY LGDIDFRELP
SCTVSNYILL AFTILIAAAV VAKFIAALQL GTKRMPELRD KFVICQVPCY TEGEESLRKT
IDSLATLKYD DKRKLIFVIC DGMIIGSGND QPTPRIVCDL LGVDPSIDPD PLLFQSVSEG
SKQLNYGKVY SGLYEVDGHV VPYVVVAKVG KPSERSKPGN RGKRDSQILL MKFLNRVHFD
APMCPLELEI CHQIKNVIGV DPQLYEFLFT IDADTEVYPD ALNRLVSAAS DDGRIIGICG
ETKLSNEKVS WWTMIQVYEY YISHHLSKAF ESLFGSVTCL PGCFTLYRIR SADKGRPLVV
SNIIIDEYAE IHVDTLHKKN LFSLGEDRFF TTLLMKHFPH YKTKFIPDAT CMTAAPETWA
VLLSQRRRWI NSTIHNLGEL MFLEDMCGFC CFSMRFFVML DLVGTVILPS TTIYILYLIV
IVSTKQAAIP IVSLVIIGAV YGLQVVIFLL KREWGLIFWL IIYLMAYPIW SFFLPIYSFW
HFDDFSWGNT RMVVGEGKNK KVLADTEDVA FDPSVIPLRK FSDYQAAMWD EDAKTSQAGY
GRRPESVGGF SMASRPMNAM GMMGGGAPGS VMGGGTNARS TMYGMNLATP GSYNRSDSRS
PSQRGSMRPN DFGGYQPGLN QHQSMLSLGG GMRGPPHQGG HMSIFNGVGP PGGGNGSVRG
SMMDFMGGGA PGTATPGLYM GGAGYPSMMP MGGGASMADM QHARNMSMFS MGGGIMPGNP
SMMMGGGGMG TPSMMMMNPM GGGMMGGGNP SMMMGGGNPS MMMGYNAGQQ QQQQQQQVQP
LTKNFNEEPS EDEIVNTLRI YLSQQDLMKI TKRSVREALN DWFPNANLNE KKPFINAQID
KILAGNS
//
