ID A0A109FGX2_9BASI Unreviewed; 1961 AA.
AC A0A109FGX2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 28-JUN-2023, entry version 38.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=RHOSPDRAFT_34213 {ECO:0000313|EMBL:KWU44200.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44200.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44200.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44200.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KQ954481; KWU44200.1; -; Genomic_DNA.
DR STRING; 1305733.A0A109FGX2; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 2.
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 PRINTS; PR00193; MYOSINHEAVY.
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 Initiation factor {ECO:0000313|EMBL:KWU44200.1};
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 Protein biosynthesis {ECO:0000313|EMBL:KWU44200.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 932..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1239..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1627..1654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1660..1681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1688..1711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..784
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 995..1057
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1902..1958
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 604..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 126..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1961 AA; 216845 MW; F3E4A95F98BEDC0A CRC64;
MAQNPFQTAA PGEEVELDPL ACPDLADLPD GVPCLSVEDL VPFFRARLLE GIPYTQISPR
VVVAVNPYQP IHATSDRALV DWRSEYADLG TEGIRGTLGP HVWAIAQKAY YHMSRTGQDQ
AIVLTGETGA GKTESAHLIT KALLNLAAPS PGKKGAKLTS SIPAATFILD AFGSASTLAN
NGASRYGRYM ELQFNDKGRL AGLKGLEYSL EKSRVANTPS GERNFHIFHY LLSGAAADER
QHLQLHSASA SFFRFLSRSR ASGHSNQADA IRFGQVKEAF KAVGFPKKAV ASIFQVLAAI
LHLGNLEFAI DRNRNADSAI VKNPHVLATA AELLGVESAE LEDALTNKST VVGGEVCAVF
LDAEGAASNR DDLASSLYGL VFSWIGEFLN EKLCKDDFAT FISLVDFPGP VHGADREGLG
VEAFCTNLAS ERLQGYVLEQ LYEANKAEYV SEDLALPGLQ TKHVSNSETV RLLTNMPGGL
VHIIDDQSRR RGKTDTTMLQ AMCKRWGNHP SFAARNGDEA QGRPGAFIVS HWDSQTTYST
ENFLAQNAAA ISPTFVTLLG GADARPGRAQ SIGQSGSTFS FVRQLFANGA LNVESHARSE
NTLVAASQKA GPRRAPSTRR PKGHSPFGEQ AGEGAGDEAT LAETPEQHHS VVKDVNDSIS
LLLNTLSTSK SWFVLCMRSN DAQLPHQVDA KLLKHQLRAF GIADLARRLR GEYSVSLDTK
EWWERYSRIP VLADEQSSLG SLTYRDKAER VREILGFSER ELGIGKTKIY LSDAAFRYLE
DFLRAEDPEE QAYLQELLSR ATTAMPATDP YALQNAPSTP ALGEYNDAYA MTSSTAALPL
VGYRQEYDYE DEAGYDSDRK AYLAGEDDYA VNTGRQVPDE EQSLAPSAYT STRPMFDARN
APEKSEMSSK LDDGVGRETV EVIRMSKARK RWVALTWLFT WWIPSPLLSW CGGMKRKDVR
MAWREKLLIN MLIWLLCGAA VFVIAVMGRI ICPTQHVYNT EELNDHSYQN DQSHMLVAIR
GEVFDFSSFA PHHFPGPSVI PTTTIEKLGG QDLTDYFPVQ VSALCNGVDG TVSPWVTLEA
TNVSTAVHQV AQYHDFRAFT SDSRPDWYYE TMIYLRYNYR KGFMGYSPGT VKSEVKKHGY
NMAIIDGNVY DFTTYIQNNG GGLQVPDGAT PPDGTSRLFM SEAIVDLFRQ KAGNDVTSDF
NRLNLASDVV QRQQICMRNL FFIGKVDTRD SAKCQFSQYL LIALSSFMVV IVAAKFLAAL
QFGRKRKPED YDKFVICQVP CYTEGEDSLR ACLDSLTKLK YDDKRKLLFV ICDGMIVGSG
NDRPTPQIVL DILGADTSVE PEALSFQSIG NGDKQHNMAK VYSGLHEAGG HIVPYIVVVK
VGKPTERHRP GNRGKRDSQM LLMRFLNRVH FDSPMAPAEL EIYHQIKNVI GVNPAFYEYL
LMVDADTTVD PFGLNYLVGG FVEDRKIIGL CGETSLVNAR ASWTTMMQVY EYFISHHLTK
AFESLFGTVT CLPGCFSMYR IRTLEHRPVI ISDAILAEYG ENKVETLHVK NLLSLGEDRY
LTTVILKHFP QYKTKFTRFA KAKTIAPDEW KVLMSQRRRW INSTIHNLVE LLQIDRMCGF
CCFSMRFVIL VDLASTLISP VTVAYIIYLV YMVVGEHKPI PTFALIMIAA IYGCQVVIYV
LHRKFEHIGW MLLYILAIPF FSFVLPLVSF WQMDDFSWGS TREIVGEQGK RLLIHDEGKF
DPASIPLQKW TDYEEALWQE GDNESIGEII EASKQQQAQE AASAYGLPYG AASVHGGGGG
YDTSPFRSGE FAPNAGAGGG YAPSVAALSQ HEMMSLQGYQ PPMTMMGGGN KRESTTSFFA
ANAIRQAAQM QQQHQQPRYS TYSQSHDQLF GGNGAAGGGG GLPSDEQLAH DVQELLSTAD
LTQVTKKRVR EALEERYGVA LPADKKALVN QVIAQVLGLD S
//
