ID A0A0F4YRT0_TALEM Unreviewed; 1982 AA.
AC A0A0F4YRT0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=T310_5039 {ECO:0000313|EMBL:KKA20954.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20954.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA20954.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20954.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:KKA20954.1}.
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; LASV01000217; KKA20954.1; -; Genomic_DNA.
DR RefSeq; XP_013327566.1; XM_013472112.1.
DR STRING; 1408163.A0A0F4YRT0; -.
DR GeneID; 25317386; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR CDD; cd14879; MYSc_Myo17; 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 SMART; SM01117; Cyt-b5; 2.
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:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KKA20954.1};
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:UP000053958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKA20954.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 893..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1599..1620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1626..1647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 956..1016
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1795..1850
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1982 AA; 220676 MW; 27EE4893D9364967 CRC64;
MALHSMSGST PSHAQSSLPS LPSHLQSDTH LTAHLASRFH VSLPTARLSS QALICINTYT
TSTKGPDGGK EGSAMAEAED LAKRAFTRLG ARGENQAIVF LGESGSGKTT IRSHLLSSFL
SFSSTPLSTK LSYAAFVFDT LTTTKSVTTP TASKAGLFFE LQYDASSSVN PTLIGGKILD
HRLERSRITS VPTGERSFHV LYYLLAGTSA AEKAHLGFES NTGGASSSHK RWRYLGHPTQ
MKVGINDAEG FQHFKTALRK LEFPRSEIAE ICQILASILH IGQLDFVTGQ ATTTTGQESG
GYSHEGGETV TMVKNKDVLA IVAAFLGLST EELEVSLRYK SKTIHRERVT VMLDPKGARQ
NADELARTLY SLLVAYVIES INQRICAAED SIANTISIID FPGFAQTSPT GSTLDQLLNN
AATESLYNYC LQSFFTSKAD LLESEEVSVP ATSYFDNSDA VRGLLKQSNG LLAILDDQTR
RGRSDHQFLE SLKKRFENKN PAIVVGDTKT VMPGSNFSSP SARASFTVKH FAGEVEYPVN
GLIEENGETI SGDLMNLINS TRSDFVRELF GQKALQKVTH PKEKTAIMQA QVSSKPQRMP
SMARRKIGPP SRFASNGARS DNEEVEDFDS QGDSVKQGAS GRRKSTNLLG PEQGAAGQFL
SSLDIINKCL TSTNLNPYFV ICLKPNDRRI ANQFDSKCVR MQVQTFGIAE ISQRLRNADF
SVFLPFAEFL GLAEAENIVV GSDREKAELV LDEKKWPSNE ARVGSTGVFL SERCWADLAK
LGERVLPVYT SDTMDEGGDG LLQPHGAYSD SKVRLLNSVD NSPTGAYIYG DETKQAYFGS
RDIDGRSDAG ASAFNSGDMF KNLETREQMA EKGNERQMEE VDSVPVSGSR KRWLAIVYML
TFWLPDFAIK FFGRMNRKDM RVAWREKLAI NMIIWLSCGI AIFFVVAFPG LICPRQYVYS
AAELASNNGK NGHPSYVAIR GVVFDLGSFI PQHYPKGLIP EKQLEQYAGT DITGLFPVQV
SALCQGTTGE VDPTVQFDYS PTNVSGSATV LSSTAANSVY HDFRYFTNDS RPDWFAEQMQ
MLRASYFKGY MAYSPQYLTT LANKQMSIAS INGNVYDFTS YIAGGRRTVA PIGKKVPPGV
NTDFMDPNVV ELFAQKSGQD VTKYWNNLKL DPGLRQRMEL CMNNLFFVGK VDTRDSAQCQ
FARYFILAIS VMLCLVITFK FLAALQFGRK NLPENLDKFI ICQVPAYTED EESLRRAIDS
MARMKYDDKR KLLVVICDGM IIGQGNDRPT PRIVLDILGV PETVDPEPLS FESLGEGMRQ
HNMGKVYSGL YEVQGHIVPF LVVVKVGKPS EVSRPGNRGK RDSQMILMRF LNRIHYNLPM
SPMELEMHHQ IRNIIGVNPT FYEFILQVDA DTVVAPDAAT RMVSAMVDDT RIIGVCGETA
LSNAKSSIIT MIQVYEYYIS HNLTKAFESL FGSVTCLPGC FSMYRIRSVE TGKPLFVSKE
VVDAYAEIRV DTLHMKNLLH LGEDRYLTTL LLKHHPSFKT KYLFRAHAWT IAPESWAVFL
SQRRRWINST VHNLIELIPL QQLCGFCCFS MRFIVFIDLM STIIQPVTVA YIAYLIAWLV
IDTSVIPFTA FVLLGAIYGL QAIIFVLRRK WEMIGWMIIY LLAMPIFSLA LPLHAFWHMD
DFTWGNTRIV TGEKGRKVII SDEGKFDPSS IPKKKWEEYQ AELWEAQTQR DDRSEASGYS
YATKSYHPGG SEYGFPATRP ASQLDLPRFG SRMSLAPSEM TGRPMDMEMS DMAGLPSDDA
ILAEIRDILR TADLMTITKK AVKAELERRF GVNLDAKRAY INSGGFPFNS EDGWMDGTVL
SELGNKLVYY LLLLIVSCRR PVSLSQLGRY LVIINRFIPI NNNKTSVEVK VNTNATSNRI
LISNVQAFCL SVCLASGPAK QQTENKKKVN NYLPTCYVSG HLDGNISWYQ CTYRQKRKQT
KK
//
