ID A0A1V9Z9M3_9STRA Unreviewed; 1458 AA.
AC A0A1V9Z9M3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=THRCLA_08121 {ECO:0000313|EMBL:OQR94669.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR94669.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR94669.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR94669.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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 -!- 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:OQR94669.1}.
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DR EMBL; JNBS01002170; OQR94669.1; -; Genomic_DNA.
DR STRING; 74557.A0A1V9Z9M3; -.
DR OrthoDB; 89602at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
DR CDD; cd04190; Chitin_synth_C; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF9; CHITIN SYNTHASE 1; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR Pfam; PF04212; MIT; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Transferase {ECO:0000313|EMBL:OQR94669.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 575..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 759..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..205
FT /note="MIT"
FT /evidence="ECO:0000259|SMART:SM00745"
FT REGION 14..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 160880 MW; DA2FAFFEA0DAA5D6 CRC64;
MSDKLDLTAR LRALREGNTP AEAPNTQQTQ RPRPLYTQDS LEFGGMYATG SPVGAEASDS
SFAQVPVWKD SKETKSYLDD EPTPQPASLL NMASNLVQRQ ASNQSFLRQN TANFRPLPNT
VEELLDGAPT YESAFRLVQL AVQMEQDGDP VAAINLYVDA GTTLVEVGKR EVDPLLQKGI
QQKAHELLQR AEDLDKWMNT VAEEARKAAL PPQLKIARTN VPTVQNAWNG RTPPFHDADE
FRLMRYTAVA TKDPIQFTND GYVLRVHQLQ RNIKVFITIT MYNEEGSELL GTLTGLAKGL
AYMCKEYGAN FWQQVAVAVV SDGRTKASKT CLEYLNGLGA FDEEIMTVTS LGVDVQMHLF
ESTLQLVENL NFENYYPPLQ LIYALKENNG GKLNSHLWFF NAFSEQLNPK YTVLVDVGTI
PAETSVFRLI RSMERNYQIG GVAGEIAVEK PNYFNPVIAA QHFEYKISNI MDKSLESVFG
FISVLPGAFS AYRYEAIRAV KGVGPLPEYF KSLTSTTKEL GPFQGNMYLA EDRILCFELL
ARKNKQWTMH YVKDAIARTD VPETLVDLIK QRRRWLNGSF FAGLFAIGHF SRVWSQSSHS
LGRKLVFTFQ FFYLALQNLL SWFLLSNLFL TFYFVLTLAF TDSAPALLQA MLTIYLAIVG
GLIVFALGNK PEPRTASFYL FSCLYMGIIM MLVTGISIYG LVGKGVSSVK DPRNITGALG
NCTVSEGELV GGVVSSLGLI FLSAFVHGEF NVLLSTIQYF FMLPTFVNVL GIYAYSNLHD
LSWGTKGLES GGGHGPTKSG NGNVKDVVEQ QKKLEAIRQA AAKEKEDVDN SFRAFRSTLL
MAWLTTNGIW LYFVTDYMSS GCYLKGLSYA VGFFNVIRFT GCVIFIIFRI IRRFGLNCCT
NGAANDTFER NLPPDWQTHY NVQNQGNGRV LMPRTDSQVP TTPRSAAAIA ATAGAVALSI
VRSNREQQEE VKQHSIIVID IGSSSVRASA YVFLNDEWIC IKGSLHQHTM QALSADGTAN
FQAIRSAVER VVDATLQWLN GKGGFNVVAL GFSSFAMSFV GVNEGGTPVT RVYTYAGQSS
VQAAELQELL QGQAAETYNR TGCPIHPAYA APQLFKQKDK VHRWQSVVGA ILTAWTDEQV
PMSYSEASWT GLFNFRELQW DEKLLKLIQL DPSTMPNIQD PSISIGGLNK KYTRRWPLLN
NAEIYLALAD GAAANIGSKC SISSRIGLTI GTSAAMRVMF PIEKISNQKV PKGLWCYRVD
SEHVLLGGAL TDGGSLYQWG QKMHSLPTDF PKQLAAMPPA SHGLIILPFL HGERAPGWHP
KATCTISGIN AATTPVHIMR ATLESVAFRL AAIYSLLSPY ASNDATIVAS GTALTASAIW
RQIIADAIGR RVSLEVDAVE TTSRGVAMYI GALNGLGSIK QPPALSSSTV DATPVLQAHS
VYLSARQEQE DLYHKLYD
//
