ID CHSA_EMENI STANDARD; PRT; 1013 AA. AC P30584; DT 01-APR-1993 (Rel. 25, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Chitin synthase A (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl DE transferase A) (Class-II chitin synthase A). GN Name=chsA; Synonyms=chs2; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGSC 89; RX MEDLINE=95072312; PubMed=7765508; RA Yanai K., Kojima N., Takaya N., Horiuchi H., Ohta A., Takagi M.; RT "Isolation and characterization of two chitin synthase genes from RT Aspergillus nidulans."; RL Biosci. Biotechnol. Biochem. 58:1828-1835(1994). RN [2] RP NUCLEOTIDE SEQUENCE OF 303-491. RX MEDLINE=92115692; PubMed=1731323; RA Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J., RA Robbins P.W.; RT "Classification of fungal chitin synthases."; RL Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992). CC -!- FUNCTION: Plays a major role in cell wall biogenesis. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl- CC beta-D-glucosaminyl)}(N) = UDP + {(1,4)-(N-acetyl-beta-D- CC glucosaminyl)}(N+1). CC -!- SUBCELLULAR LOCATION: Plasma membrane-bound. CC -!- SIMILARITY: Belongs to the chitin synthase family. Class II CC subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D21268; BAA04806.1; -. DR EMBL; M82939; AAA33303.1; -. DR PIR; JC2314; JC2314. DR InterPro; IPR004834; Chitin_synth. DR InterPro; IPR001173; Glyco_trans_2. DR Pfam; PF01644; Chitin_synth_1; 1. DR ProDom; PD002998; Chitin_synth; 1. KW Cell wall; Glycosyltransferase; Multigene family; Transferase; KW Transmembrane. FT TRANSMEM 508 528 Potential. FT TRANSMEM 646 666 Potential. FT TRANSMEM 686 706 Potential. FT TRANSMEM 721 741 Potential. FT TRANSMEM 759 779 Potential. FT TRANSMEM 892 912 Potential. FT TRANSMEM 919 939 Potential. SQ SEQUENCE 1013 AA; 113679 MW; DD5D2E9523B0778A CRC64; MDCQNGRRAN RTVRFARTAE SRYPERYSYE YDPEETLSRA APSMRNAPTI PPPTASGADE MRYTASRPAS PARPWSPTRA ADWVRPPSAA ASYYERADIN GSPRPGTPSS RYGGSPRRPL PPAPLFSKPG TTTQDTKIDI GDGEEDPFGG GGRTISSRHG PQGSVQSFTS ESTFIADETD LEKVDLDEYE EESNETKSMV DPNLHYGPAP EKQSRRGVRN AQMAKKEVQL VNGELILECK IPTILHSFLP RRDDREFTHM RYTAVTCDPD DFTQRGYKLR QQIGRTMRET ELFICITMYN EDETHFTRTM HGVMQNISHF CSRSKSRTWG KDGWKKIVVC IISDGRKKVH PRTLNALAAL GVYQEGIAKN VVNQKQVNAH VYEYTTQVSL DSDLKFKGAE KGIVPCQVIF CLKEHNQKKL NSHRWFFNAF GRALQPNICI LLDVGTRPEP TALYHLWKAF DQDSNVAGAA GEIKASKGKN MLGLLNPLVA SQNFEYKMSN ILDKPLESVF GYITVLPGAL SAYRFFALQN DAEGNGPLNQ YFKGETLHGK DADVFTANMY LAEDRILCWE LVAKREERWV LRFVKSAVGE TDVPDSIPEF ISQRRRWLNG AFFAAVYSIV NVKQLWKTDH SLARKILLQI ESVYQLLQLI FTYFGLANFY LAFFFIAGSL TDEKIDPFGH NMGKYIFIVL RYACVLVMCL QFIFSMGNRP QGAKKLYLSS MIVYSIVMAY TAFCTLYLIV LELMAKTGHD VPITMSDTLF VNIVVSLLST VGLYFFTSFM YLDPWHMFTS SAQYFALLPS YICTLQCYAF CNTHDVTWGT KGDNTINTDL GTARIINGSI VEVEMPSEQL DIDSGYDAAL RNLRDRLEVP DPGVSESQQQ EDYYRAVRTY MVSVWMVANV VLAMAVSEVY GVGSSGTNVY LAIILWSVAV LAIIRAIGST AYAVLYLIQK LVEGKAKFQA GNIASANASA AGSSLGTKSN VSYGSKGLNM TDRINETKWA ISRGMQKAMF WKK //