ID B6Q766_TALMQ Unreviewed; 1854 AA.
AC B6Q766;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PMAA_035260 {ECO:0000313|EMBL:EEA28731.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28731.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; DS995899; EEA28731.1; -; Genomic_DNA.
DR RefSeq; XP_002145246.1; XM_002145210.1.
DR STRING; 441960.B6Q766; -.
DR VEuPathDB; FungiDB:PMAA_035260; -.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OrthoDB; 1331060at2759; -.
DR PhylomeDB; B6Q766; -.
DR Proteomes; UP000001294; 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; 1.10.10.820; -; 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 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:UP000001294};
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 891..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 931..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1203..1222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1598..1619
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1625..1646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1653..1676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..784
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 954..1014
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1796..1851
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 581..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..646
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 1854 AA; 205873 MW; E4AAF3A13C658292 CRC64;
MALNSFPGST PSHTQSSLPS LPSHLQSDTH LTAHLASRFH VSLPTARLSS QALICLNTYT
SSTKGPDGGK EGSAMGEAED LAKRAFTRLG ARGENQAVVF LGETGSGKTT VRSHLLSALL
SFSATPLSTK LSLAAFVFDT LTTTKSVTTP TASKAGLFYE LQYDSSSNNP LLIGGKILDH
RLERNRITSV PTGERSIHVL YYLLAGTSAA EKAHLGLESS GIHAGPGNNQ KRWRYLGHPT
QLKVGVNDAE GFQHFKTALR KLEFTRGEIA EICQVLATIL HIGQLEFITG QSTTTSAEES
GGYSHEGGEI VTMVKNKEVL EYVAAFLGLS TEDLAVSLRH KTKTIHRERV TVMLDPRGAR
QNADELARTL YSLLVAYVIE SINQRVCAAE ESVGNTISII DFPGFAQSAN SSTLDQLLNN
AAVESLYSFA LQSFFSNKAD RLESEEVSVP ATSYFDNSDA VRGLLKTGNG LLAIIDDQTR
RGKTDLQMLE SLKKRFQNKN PAITVGDSET KLPGSNFVTP STHATFTVRH FAGEIDYPVN
GLIEENGETI SGDLINLISS TRSDFVRELF GQDALQKVTH PKERNAVVQA QVSSKPMRMP
SMARRKISPS SKLNPFSNRA GRDDDDSDSN NGSTKTGNTS RKKTNGAGAD QGAAGQFLAS
LDVIKQCLNA PNLNPYFVFC LKPNDRRIAN QFDSKCVRLQ MQTFGIAEIS QRLRNADFSV
FLPFAEFLGL AEAESIVVGS DREKAELVLD ERKWPGNEAR VGSTGVFLSE RCWADIARLG
ERVLPTYHAD SLNDGDGMLH PQGSYSDHKV RLLSSGENSP SGAFIYGEES KQGGYFGSRE
IDGRSDAGAS AFNSGDMFKN LETREQMAEK SKERKMEEVD ILPVSGSRKR WLFIVYLFTF
WVPDFLIRFL GRMKRKDVRM AWREKLAINM IIWLACLTAA FVVVAFPMLI CPRQDVFSAE
ELSSHNGKDG ASSYVSIRGV VFDLGAFVPS HYPKNLIPSS AFDNYAGVDA TALFPVQVSA
LCQGVDGSVD PSVLLDFTPV NITGSATTIS TADQNSKYHD FRYFTNDYRA DWFAEQMMML
KGSFKKGYIG YSSQYLKTLA EKNGRSVASL NGNVYDFTEY VAGGRRTLGP NNTTGPAGVS
VDFMDPVVVN LFSQRSGQDV TQRFNQLSMD PELRQRMKLC MDNLFFVGKV DTRNSTQCQF
SEYFILAITA LLASVIIARF LAALQFGKKN IPENLDKFII CQVPVYTEDE DSLRRAIDSM
ARMKYDDKRK LLVVICDGMI IGQGNDRPTP RIVLDILGVP DTVDPEPLSF ESLGEGMRQH
NMGKIYSGLY EVQGHIVPFM VVVKVGKPSE VSRPGNRGKR DSQMILMRFL NRIHYNLPMS
PMELEMYHQI RNIIGVNPTF YEFILQVDAD TVVAPDSATR MVSSFLADTR IIGLCGETAL
SNARKSIITM IQVYEYYISH NLTKAFESLF GSITCLPGCF TMYRIRSADT GKPLFVSKEV
VEAYAEIRVD TLHMKNLLHL GEDRYLTTLL IKHHPNYKTK YSFRAHAWTI APENWSVFLS
QRRRWINSTV HNLIELVPMQ QLCGFCCFSM RFVVLIDLMS TIIQPVTVAY IVYLIVWLIL
DTSKIPITAF ILLGAIYGLQ AIIFILRRKW EMVGWMIIYI LATPIFSLGL PLYSFWHMDD
FSWGNTRVVT GEKGKKVIIS DEGKFDPASI PKKRWEEYQV ELWEAQSRVD DTRSEVSGYS
YATKSYHPAA TEYGYPASRP MSQLDLTSRL GSRMSLAPSE MMGGTANYEL ADLTGLPSDD
AILAEIRDIL RTADLMTITK KVVKVELEKR FGVNLDAKRP YINSATEAVL SGQL
//
