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Database: UniProt
Entry: A6QTJ5_AJECN
LinkDB: A6QTJ5_AJECN
Original site: A6QTJ5_AJECN 
ID   A6QTJ5_AJECN            Unreviewed;      2501 AA.
AC   A6QTJ5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Myosin type II heavy chain {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HCAG_00701 {ECO:0000313|EMBL:EDN02837.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02837.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ISY1 family.
CC       {ECO:0000256|ARBA:ARBA00007002}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; CH476655; EDN02837.1; -; Genomic_DNA.
DR   STRING; 339724.A6QTJ5; -.
DR   VEuPathDB; FungiDB:HCAG_00701; -.
DR   HOGENOM; CLU_000192_5_3_1; -.
DR   OMA; QRAMDIE; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 1.10.287.660; Helix hairpin bin; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR   InterPro; IPR029012; Helix_hairpin_bin_sf.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR009360; Isy1.
DR   InterPro; IPR037200; Isy1_sf.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF06246; Isy1; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF140102; ISY1 domain-like; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT   DOMAIN          86..136
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          140..835
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..736
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1616..1654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1686..1708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2124..2155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          913..947
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          983..1520
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1556..1590
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1791..1818
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1896..1958
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        38..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1628..1654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         233..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2501 AA;  286294 MW;  27D7A9F93625FB74 CRC64;
     MDDELEVSRR RRCESLPSQV TASRPKGAHG PPHPGSGSNL LRTKQRSNSR TNLATSNTFA
     PQFIKSEELR RGADQIRGIE GDNDFSGKRY VWLSDPEKAF IKGMVLDDTQ DGHLLVQCDD
     GSQREVDSES VDKVNPAKFD RADDMAELTH LNEGSVVHNL LTRYKSDLIY TYSGLFLVTV
     NPYCPLPIYT NEYVKMYNGR SREETRPHIF AMADQAFRNL VEEGRNQSIL VTGESGAGKT
     ENTKKVIQYL ATVASSPEGS QGRLTSKQNS NLSQQILRAN PILEAFGNAQ TVRNNNSSRF
     GKFIRIEFSR AGQISGAFID FYLLEKSRVV KVNSQERSYH IFYQLLRGAD KELRHHLQLS
     EQGIEDFWYI RDGNDSISGV SDLDEWNNLM EAFSIMNFSG NDQLSILRTV AAVMHLGNVT
     VTKESLRADQ ATLTPEGYES AAKACQLLGI PIDPFVKGLL HPKVKAGREW VEKVQTPEQV
     RLALDALAKG IYERGFADLV SRINKQLDRS GTAGDDSCFI GVLDIAGFEI FETNSFEQLC
     INYTNEKLQQ FFNHHMFVLE QEEYAREQIE WQFIDFGKDL QPTIDLIELP NPIGIFSCLD
     EDCVMPKATD KSFTEKLHSL WGRKSPKYRS SRLNQGFILT HYAAEVEYST EGWLEKNKDP
     LNDNVTRLLS SSSDKHIANL FADWAEVDGE HEVSKSRVKK GLFRTVAQRH KEQLSSLMAQ
     LHSTHPHFVR CILPNHKKRP KLFDGPLVLD QLRCNGVLEG IRIARTGFPN RLSFTEFRQR
     YEVLCPLTAK GYLDGQSAAS LIVENLGLDK SLYRIGLTKM FFRAGVLAEL EEQRDTLIRD
     IMTRFQSVVR GFVQRRIANK RLYRTEATRI IQRNFHVYLD LKSSPWWTLF VRMKPLLGAT
     RTAGEVKKRD EQIKQLEEKV RNDIVERQKL EEERRRADVE VQRIRKTLES ERALALDKEE
     IFKRLQFREI ELSEKLAGAI VDQEGLEDQM DELIASKKKT EEELELRRSQ LEQAAQIISR
     LESEKKELQG QITELEKQLQ DIENNHQKRD SEVDRLSQEV KMLNSHLSLK ERKLQDLEAK
     LLKSNQNLDI KLANATKELQ FSRKQVKDLV EENRSIRQQI SDLSSTSTGY EELVRRKEGE
     ISILRGDVKK LESEKITLEA EKQTLTRRHS DMQQRLRELQ AQTDAMTSEK KNLEREAADV
     KKLLEAKISE DAEAGQCRKL LDQQIKDLKE QLNLTSLNES KITNREKKCI SPIDTLRRAT
     EARAAAEASC KELQKELINL RERFTKVERA HLDAETAIEK KIVAQASERQ ASLRRDLTAK
     SNELDEVEKE RARLAAQVQD LTRTMAESEA FRIRHDQHKE RLERELVTIK GRLAASENDN
     RALLNKIQQK NLDIARSNSR ASDTQRSRMV QIQNEKSRLE EVNKQLLRQL GDAQLSITAL
     EKQKEKLALS VEDLNHEVTR EHKATRSAEK ASSASNIQLA EANRNLETER QLRIQAQANT
     RKLQASVDQA NKELQDCHQQ LILLHKVFNP EADENPSSWE AVKPNLSKSV DMAAVLESVQ
     NKLRVTEEKC ARAESQLAEM RRRHADEMAE LDARYSSSKR ALLEEIDQNQ VAVSRSPNHF
     KKNSDPVKRY SNPCTPNNRR FNFNDGANDS GRSDRTVDTV AFQKRMDTAA EIGMLQNQLQ
     LTEMQNRQLQ SQLERSSPGR DSWQDESPSI RRMQLLEREN GRLHEKLDDS AKKVSALERS
     IQSGELTLRD VQARSHEELY DLLNSQEQSR KSLLHAHKSA LADLTDAKGQ LDKIKHSRVS
     LEVELRDATS ELKELQLARD QDAAGRSQLL QEFADLQIRL DAETSKVSDL TSSLELYKGR
     ADEYFGKLEQ AEIAVLKASR AEQFAKAQAK EAEDTCATIM AERKQMDSLI EDLQRQTQSY
     EEKVEDLAAD LDAALQAKRR LQNELEDYRS QRAMDIEDKE ISLEQTRKKY QMEFSTLTNE
     LEIEHDISNE RDALLKEKRT LEERLNEASD RLAELAQGEN PSVRNAAEID RELLELRTKL
     AQQEDLSSAA VGKMRRAEAL ATEIQKEIVA ERESNAQLFK EKAALEKQLK EAQLKCVDLE
     TKGYTSPSQD VRFLHKRIQE LETQLDEQES KRNADQRSIR NVDRTVKDLQ SQIDRRDKMN
     AQLSEDISKS RDKIERLLKT VEELQSSDSE NQLQARRAER ELREEREKSL RLERELEAWK
     GLRVERGSAT GRSGTVIGLS EVGDRFGGVN ARNSEKAQSM LFRFRAAQAA DLGILDIGRT
     RRPKAITSVT SIPVCEKWRG QVLKEISRKV SRIQDQSLSD YQIRDLNDEI NKAMREKWMW
     EVQIRNLGGP NYTRGGGRVY DDDGREIPGG GKGYRYFGRA KELPGVKEMF EAAAKKQSRR
     GKEEDTDGGG RVVDISRRHV DAAYFGYGLD EEDGTLLEYE SQKEKEAFEN MLKRGEDEAA
     DGWAPLPGDA GDGVEWRLPT LEEVQEELVD RRRRRLLDKI L
//
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