ID S2K1T9_MUCC1 Unreviewed; 1254 AA.
AC S2K1T9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Myosin I {ECO:0000313|EMBL:EPB89143.1};
GN ORFNames=HMPREF1544_04010 {ECO:0000313|EMBL:EPB89143.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB89143.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
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; KE123939; EPB89143.1; -; Genomic_DNA.
DR AlphaFoldDB; S2K1T9; -.
DR STRING; 1220926.S2K1T9; -.
DR VEuPathDB; FungiDB:HMPREF1544_04010; -.
DR eggNOG; KOG0162; Eukaryota.
DR InParanoid; S2K1T9; -.
DR OMA; AHMQFYR; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000014254; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; 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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11856; SH3_p47phox_like; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000014254};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 39..719
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 777..968
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1042..1101
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..614
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 959..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1254 AA; 140023 MW; E3E1AE7BC19CE2EE CRC64;
MKRFGGGGKK SGIGGEKKAI KANRPARADW KEGMKKRQVG VSDMTLLTKI TDEAINENLE
LRWKNGDIYT YIGHVLISVN PFKDLGIYTD DILQSYKGKN LLEGTPHVFA IAEASYHHMN
SYKENQCIII SGESGAGKTE AAKRIMQYIA AVSEGKSAAI QEIKDMVLAT NPLLESFGCA
KTLRNNNSSR HGKYLEIQFS AQGEPVGAVI TNYLLEKNRV VGQIENERNF HIFYQLTKSA
PVEYKEQYGL QGPESFLYTS RSHCLNVEGI DDVKDFQDTL QAMDIIGLQP AEKDDIFKML
SVILWLGNVV FAENEHGHAV VTDADVVNFI AYLAQVEYAD LDKALTVRIM ETQHGGRRGS
VYEVPLNVNQ ATSVRDALAK SIYERLFEWI VTRVNVSLQA RGDVRHTIGV LDIYGFEIFE
NNNFEQLCIN YVNEKLQQIF IELTLKAEQD EYVKEQIEWT PIKFFDNKVV CDLIEAKRPP
GIFAALNDAC ATAHADPEAA DNSFVQRLGF LASNAHFEAR GSQFLVRHYA GDVYYNIAGI
TDKNKDALLK DLLDLAASSK DLFISSILFP ERIDPNSKKR PPTASDKIKF SCNALVEKLM
MCHPSYIRTI KPNDNRSSTE YNVQRVHHQI KYLGLCENIR VRRAGFAYRT VFDKFVERFY
LLCPATGYAG DYIWQGDARS GCLEILKHNH IPADEWQMGT SKVFIKHPET IFGLEGLRDK
YWHNMATRIQ RAWRAHVRYK NECATKIQRF WRGNKHNIGY LQLRDYGHQL LGGRKERRRF
SLVSQRMFLG DYLDVQNGSG LATMIRNAIN LKPGEQVLFS MKGATLVPRA MRSSVPSPRT
FIMTNQNFHI VVTTKNGKAI QMVDEKVLSL NTIRNASVST LRDDWVVLHL DSSPDGSDCV
ISCVFKTELL ARLSQATNGR ITVNVEPQIQ YKKKGGKIVT MKFIKDEKIP RDDFYKSHVV
HVPSGEPPNS QSRPPVARKS KLPSINQQRQ PARKHTVNSI PQSIAAPKSD YTSNVNNGNQ
AGSSFPAPPI TTSQPPAPAV PSKLPLYKAI YPFQSQEGGE VSFQKGETME IVEKDQNGWW
LARINGKDGW VPSNYLEECV APKPSPPPPA RRRAPPPIPQ EQQNAQQPAS ERQPEPASAV
NHMSGPTTNG IPAWRAALNA KNASAHNTVN DTTTPTPASR GPPVPAKPSV PGSRPTPSNP
LAGRLAPSIP GRPQAAPSPQ APPRNSSPAA LSLADAIKAR RQQAPQSDDD DEDW
//
