UniProt: A0A162V9E6

Database: UniProt
Entry: A0A162V9E6_PHYB8

LinkDB:  A0A162V9E6_PHYB8 
Original site:  A0A162V9E6_PHYB8

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (3)   
   SMART (2)   
All databases (27)   

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ID   A0A162V9E6_PHYB8        Unreviewed;      1811 AA.
AC   A0A162V9E6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=PHYBLDRAFT_17470 {ECO:0000313|EMBL:OAD81043.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD81043.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-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; KV440971; OAD81043.1; -; Genomic_DNA.
DR   RefSeq; XP_018299083.1; XM_018437321.1.
DR   STRING; 763407.A0A162V9E6; -.
DR   GeneID; 28998227; -.
DR   VEuPathDB; FungiDB:PHYBL_17470; -.
DR   InParanoid; A0A162V9E6; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000077315; 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   CDD; cd04190; Chitin_synth_C; 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; 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   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:UP000077315};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        836..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        871..895
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1144..1163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1533..1556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1568..1587
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1594..1617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..737
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          899..957
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          1755..1810
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          575..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..635
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          740..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1811 AA;  205074 MW;  9C77B24BC6F2456F CRC64;
     MTQSSHITDL VQLSPDPSPN DIAEVLRQRY LNDHFYTSIN RAVLIALNPY KLHDGPLAST
     SADYVAEYKD TQCAKANQWR EPHLFQLVNH AYFHMRRTSI NQSVLFSGES GSGKSERFRQ
     AVGHLIALST HKKQTRLQQH LQSSQVLLDL FGNAKTTVHD NASRLAQYLE VHFTERGRMA
     GAKFMPYALE KYRVTMAAPD ERNFHVFYAV LSGASPEEKA RLGLSDWTAY HYLARTSTAR
     ASSIDDSQNY VNLRAALKTL LFHKHTVTQL FQVLAAILHL GNLVFIEDPN NAQDAAIIKN
     MDALTTAADL LGVDPKALMS TLTYKSKLIK RDITTLFLDP AQATIQRDEL AQTLYVLVFT
     WLTEQINDKL SAKEGSHSLI GLLDTPGMTA VRTTAHASFD QLAFNFITES IHQFMLSSLF
     ERDVHEYAEQ GVPMPMEAWP TNTATVDLLV HPAKGLFSIL NTQANRQGSR PTDDVLLDQF
     ANANRSSSDG ILLSFKKSDT GARLFAIQHF WAQTTYDPRG LMDRNEDYLC NDFIALFRGN
     AYSAPTTNGL VASLFNEPMI EEDYSIRNRV SSPQLGIRPL QSPTNLDKSD DKTASRLSDS
     SVPTVVDQLM NGITDLTQAL SNTIPWFVLC MRPNELSLPN SCDAKKVTVQ ISSFRLTELI
     RRLRVSYNTI FPMDEFFDRY GIALTMLLGQ SIEAGTLKER CKLVVHALGW NETYAGIGRD
     KIYLSNNAFR ILEDELRSTE KSDSKKTKIP TGGMSLRHRR DNFDGYSFND DQVSSAMSND
     DFLDEASPVN DFHASDLFSP SQSDPTEIER KAEYPPPGEP EHEDEQDQIS SERRKWLILV
     WGLTWWVPSP CLQYCGGMKR KDIRLAWREK LALCILIFLL SASMVVFIVF FGPLICPQQD
     VYSFSELQSK SEKQSAYVAI RGEVFDLTKF APHHWASEVI PDSTLFDYAG KDATNLFPVQ
     VSALCDGTTG VVSDEIVLDF QANLTDRNAA YHDFRFFTND YRPDWYFEQM VYMRKNYRLG
     FMGYEPSDIL RQATNVVSVG DISTHRQWAI LHGDVYDLTY YLMGGRAPRA PEGQMPPPNL
     DLNFMDNTII ELFRQLAGTD ISAHFDALPI EKELRTRQLV CLRNLFFVGK LDTRRSIQCQ
     FAEYFLLIIT GFLCTVIVFK FIAALQLGAF REPEDYDKFI ICQVPCYTES EESLRMTIDS
     IAVLRYDDKR KLLFLVCDGM LVGSGNDRPT PRIVLDILGV DPNIDPEPLS FLSLGDGMKQ
     HNMGKIYSGL YECSGHVVPY VVVVKVGAPS ERQKPGNRGK RDSQMVLMRF LNKVHFESAM
     TPMELEIYHQ IKNVIGVNPS FFEFVLMVDA DTEVMPESLN RMVSCFVHDS KIIGLCGETA
     LSNEKDSWVT MIQVYEYYIS HFLAKAFESL FGSVTCLPGC FCMYRIRSPA KNQPLLVSNQ
     VIEDYSENKV NTLHQKNLLH LGEDRYLTTL ILKHFPTYKT KFTADASCLT NAPDRWSVLL
     SQRRRWINST IHNLGELIFL PQLCGFCCFS MRFVVILDLL STLAMPAVVC YLGYLIYRLA
     TNAGQVPMIS IITLGGIYGL QAIIFIVRRK WEHIGWMIVY ILAIPIFSFF IPIYSFWHFD
     DFSWGNTRVV VGEGGQKKAL PVDEGRFDPK TIPLKKWSDH ENEIWESGSI ETKVTAVTAT
     SRRTFGSPAP PAYPPYPASV KGGPATVYND AASFRYSPAH LRAPSVLPPL QLPMMSSPSL
     YSDVASGYHE PYLNGPTDDE IRREVQRITA SADLMTMTKK QVREQLSRHF GIDMAYRKDF
     INYCIEEALH F
//

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