ID A0A1V8UGE9_9PEZI Unreviewed; 2194 AA.
AC A0A1V8UGE9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=B0A51_09723 {ECO:0000313|EMBL:OQO22785.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO22785.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000256|ARBA:ARBA00024009}.
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:OQO22785.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NAEU01000450; OQO22785.1; -; Genomic_DNA.
DR STRING; 1974281.A0A1V8UGE9; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding 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; 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 SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 2.
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.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 736..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1034..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1425..1448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1486..1509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1708..1764
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1646..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2194 AA; 244731 MW; 288230BD47824345 CRC64;
MANRNSHFST MSGPAQGRAG TMQGASQQVS TTTLLNALHN SFSLGQPYPL ESSTSLVVNT
WLSASQTGAD GRVGGTVDTE LARRSWEHAR RRAEDSTIVL GSLHRSTPSA FAPFISALPI
SVPGSFYTAL NALRPFLHTA TPFNPSFARY SALSAAFTLN LTGEITGAVL SLSTSGIDTQ
EGLLNVPAES GYRAFDVFYY LLTSASSVQE REYLGLKAPS RYALLRRSET YDPPSYLPTA
DDTAAAEDFR ESLKAIGIKG KSLRSLLSVV AALLRLGDAL GFLIDEEELE STCEEVAELL
EINPDVLIKK CATEEREILI AAVYESLVDW VITKANEAVR HELHNGRTIG SSNGSDAGMH
TPPSSQDDGD TVGITVVEVP SSTLGKAISL KTIFDDSTGI NLEMKEDGVP IVPAGSSVIR
EMKDAVQISS ADLEAMDTPA VREREDQLDR RHTALEKVGA EIEEDSFLKG ILYPVTGNGI
VLGKTGRFSL SNLLGTSRVW FQLALHPSDD FPATLAQQGP QAFPWSAGSV SSQIRAWRLP
EWANYRTKQL DFTADFDHEE FVERYNRLGC QAGRDGVESF ILERGWSNGE VVVGNERVWI
REPAWWEAES MLDMKPEEPS DMLGGMVGAA GMENGYAVQT PNGVENPFFG GSQYGDSRDN
LLSVAPSAMA PSRMGARSLA PTHAQTIRSI SGGDYGLGYK GDDNKGGVTY YGQELDPELA
EGKHIQEETV PFSRRMWVWF VWAMTFWIPS FVLAHVGRMK RPDVRFAWRE KLCLMFLIAL
MNGTIIFWIV GLGNLLCPNW DKAWSPQEVA YHTGDTDWWV SYHGDVYDLT KFWKLQHSDN
NIETTSDNME PFAGLNMDDY IVPPLTIACP GLVTDINVIM TPNETLLNPL GAHISGPTFQ
SDSTTKLNSI NWYTEYFLPR MKEYYKGARV IKKSVVKSDG ENNNHQWVII ENKVYDLTNY
FYTLKLQNNL PQYSFFPDDV NQLIQENPGQ DITENWNTQI PYANRTNSMN CLNNVFYVGQ
TDFRDTAKCQ VNNYLLIVFA GILCSVILVK FLAALQFGSR RKPGQQDKFV ICQVPAYTEG
EDSLRKGLDS LTALAYDNKR KLICVICDGM IVGGGNDRPT PKIVLDVLGV DPKVDPPALP
FRSVGVGNEQ LNYGKVYSGL YEFEGNVVPY IVVVKVGKES EQTKSKPGNR GKRDSQILLM
SFLNRVHHRS AMSPLELEMF HQINNIIGVD PELYEYLFMV DADTKVKEDS LNRLVAACAN
DSKIVGICGE TSLENEERSW WTMIQVYEYY ISHNLSKAFE SLFGSVTCLP GCFCMYRIRT
ADKGRPVIIS NKIIDEYAVN NLDTLHKKNL LSLGEDRYLT TLMTKHFPNN SFKFVPEAYA
LTEAPSEWSV LLSQRRRWIN STIHNLAELV FIKDLCGFCC FSMRFVVFID LMGTIILPAT
CAYLAYLIYR VASGTGQFPL ISIVMIAAVY GLQALIFIIK RQWQHIGWML IYILAYPIYS
FVLPIYSFWK QDDFSWGNTR VVLGEKGNKQ VVAVDDEGFN PKSIPLQRWD DYATANNLPG
RRGIPTEKEG GSAMYQDGGY EMDDIRSTYS SIKPASTILG HFPQQQRHRP PQSPSPYAAL
NRQSTYSRYT DLANPGTAEQ QRLMSMGGMS DYPHPQPVSR HHSTDALNQM RQPSPLGTPN
PSASPYGYAS QSRPQSTANL AAFTVGPGPT NEAIAACVRE CLGEVDMDSV TKKQVKALVE
QKLQCQLSGE KRAWLDERID WELSNIINVA TIWSTMAFVA NAASTPKRKL TSGQFAWPRP
KRPATCQLDL TQDDNEESDE IEIPAAYIGD AGKEPLLFPA PKTALSKSEM ALRERKCEER
LLQACKRLEA ERADFSPRFA KYVYTEGAEK LAKKMMLALL PAWKHVLGSD EWSMAAVEEL
AAKDLTLHAA GLYFAMCDRA GYIGSSVDLA ARLAQHVNQI VANRKGSAFA EHKLFYNYCT
EAKPKPVRFA YVAIPVEADP EFIEVMESVL ISIFGTFERG LVKSMVRQVR ITKAIRPQGL
PATPWLAGNA SLPVCMAFQE KPTEEQLEAS MKRCAEARGL WNKAQRDLLQ TRKLEAAKEA
GIALVYCEAC QIYGSKDYFT RTNKYSHKMT ETHQLNLPPE ERTERVLTEC GCGKSYDPGN
KNSHTKGKHH QKWLSEEERD GETEIWCEVC EQWQ
//
