UniProt: A0A1R1XQI4

Database: UniProt
Entry: A0A1R1XQI4_9FUNG

LinkDB:  A0A1R1XQI4_9FUNG 
Original site:  A0A1R1XQI4_9FUNG

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   SMART (1)   
All databases (17)   

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ID   A0A1R1XQI4_9FUNG        Unreviewed;      2000 AA.
AC   A0A1R1XQI4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=AYI70_g6307 {ECO:0000313|EMBL:OMJ16891.1}, AYI70_g8724
GN   {ECO:0000313|EMBL:OMJ13075.1};
OS   Smittium culicis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ16891.1, ECO:0000313|Proteomes:UP000187283};
RN   [1] {ECO:0000313|EMBL:OMJ16891.1, ECO:0000313|Proteomes:UP000187283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSMNP {ECO:0000313|EMBL:OMJ16891.1,
RC   ECO:0000313|Proteomes:UP000187283};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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   -!- 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:OMJ16891.1}.
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DR   EMBL; LSSN01003647; OMJ13075.1; -; Genomic_DNA.
DR   EMBL; LSSN01002197; OMJ16891.1; -; Genomic_DNA.
DR   STRING; 133412.A0A1R1XQI4; -.
DR   Proteomes; UP000187283; 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: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   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
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; PF00063; Myosin_head; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        826..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        860..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1131..1153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1523..1547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1553..1575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1582..1605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..752
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|SMART:SM00242"
FT   REGION          211..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1897..1937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2000 AA;  226186 MW;  C51755C588ACB247 CRC64;
     MDNSHTYVDG SPVKNFYNLN KIKDASTINV EKLAKHILDT IEAYSGTFFS VGSQVLLSID
     NSRDNPSFQN HDIASAYYEY LIAGSSPKNQ RVNLDNPHIY KLINNAYNHM LFSNQSQSVI
     FLGHAASGKS VNKLDSIFML NIMNPGQQEF FDKLNASIKV LDYFTTSRID KFNVASSRAN
     TILDIFFDSA GSPIGSKTTI LSLESNRFRD NPKSNLNKSP FLPTLNKLGN SSSPQNSPTS
     NDFPIFQIID LFKDICSSHF ISLRLDPSLD SNDSPSSSGN LDFSDLSSIG SQELIDLQLL
     MKSFGISNKL SSKVFTLLGA IVNLSSIDFV KSSSQNNVEP VSIPNGLAES LGFVRSNSHL
     SDLLTTSRSN INNSRVVTNL SVDASINKKL DLCWILYRQL VYWIVDSINN SLSTSDESLS
     FSLIDTIGSN AISSDFDLLS INFFNDRLIN FMTYEIFQSN NIEYTKENID FIPIINPNSD
     NKSRLDLYLN PNAGLFSIIE SNSSLITSSI FEKKRNFSSS RSSISNSSSF YSTNFSQSDS
     KFFLDLKNIL DLDSSHYFGF AKKSNFFEIS HFFGKSEYNS SNIIRSNVLE SKTFLDEEYR
     QLLANSNDKS FVSALFSSPE NDEPNTMCVT VSKLAQNANK LISHIESSKT WFVVCLLTNI
     NNSSLSLSNK YLISQLKSYD MDLVVRRKRT EFFISFDFDQ FIELFHHKSD DDKFIKKLKL
     HLKYGHQDFF IGKSKVFLSS ECFNNLVYLF NNNLLDLDKV INDEDPSRLS HIDKDNYGQN
     SNKKINNASS DFDSNIQLKT QSKVEKSQTS PFKKSKPKKS GMRKTWLFIV YSLTFYIPIF
     LVSIFTGIKD KQRLMAWREK VALCLIILFS CFFVIFWIGV LGLLICPKQN IYSLPELFGH
     NTEGDALIAI RGEVFDVNKY QHNGVTFKQL LDNNYLGRDL SNTFPLQLSY VCNGLNVDPR
     LSMQDKPILY SDTYYHDHRW YRHYNDKNGF NYYQYNVMRV LRSGHAHGRI GFDPKNLLVS
     SVANPKDNVY RSIINGQVFD LSSYINANGA PYIVTPDGIS NDTNTISTEA RNFMSPTVRT
     MFQQNQGKDI SDIWSTYLQS NPNEAKINFN CLRGAFYIGD VDLRKSFRCY FANYMLLAGS
     IFIVSMIFVK FIASIRIGNK KVNPELFESF VICNVPCYTE NEESLKGTID SIARMTYDDK
     RKLICIVCDG IVMGSGNDKP TPNILFDILN IANVDSEPLS YFSLGENIKQ HNMAQIYSGL
     YEVSGHTVPY LLIVKCGTPG ETLKRGNRGK RDSQILLMRF FNKVFFDLPM TPLELEIFHQ
     MKNVIGVDPS MYEYILMIDA DTTASRMGLS YLLSAMQNDS KIMGACGETQ IANPKESWTS
     MLQVYEYFIA HFMAKSFESL FGTVTCLPGC FCLYRIKSNN GQIPLLISNT VVQEYSTNKA
     VTLHEKNLLL LGEDRYLTTL MLKNFPNYKT KFVGYANCKT NVPQNWRILL SQRRRWINST
     VHNLFELILL PNMCGFCCFS MRFVVFIDLI STVIMPATMA YLGILIYQLT NTATSYISLY
     LLVAIYALQA FVFILHKQWQ HIGWMIIYLI AIPLFSFMIP VYSFWHFDDF SWGNTRKISN
     TDDDDSSGGK NKFENFEMTT FDPKSIPMRK WSDYEKELLF EMNSEAFNGR SQTSHSVNSR
     SGAQSRAATA MSYNQMAGMQ GGGPVPQFHA GQMGIGGGYP AHMSPVPQFA PNFSTIPSAP
     VSLHNAGVPM HMMNAIDPSL IRSSYNPNRL STYSQGFQMG QNPQINNMRA TNVQMGPSAQ
     MNNMQMNPIN QMGNMNMPSN QIVYQQQRTP PTPINNEQNI GIYNLGSNNV GSQPAVSNFV
     NDENAFVANL SAYMQNSTSI ASYNSNVPLL NQNQQNFSPQ KQQLSPNQNQ SRQQLSGNEN
     AGSTTFSDDG SNWPSGASDK MITDITLDLL NQNGTLELSK REIRNMISQR ANMSPEEIKM
     RKAVINNAIL EFINFHNAQQ
//

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