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Database: UniProt
Entry: A0A1S3EX94_DIPOR
LinkDB: A0A1S3EX94_DIPOR
Original site: A0A1S3EX94_DIPOR 
ID   A0A1S3EX94_DIPOR        Unreviewed;      1986 AA.
AC   A0A1S3EX94;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Myosin-10 {ECO:0000313|RefSeq:XP_012868569.1};
GN   Name=Myh10 {ECO:0000313|RefSeq:XP_012868569.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012868569.1};
RN   [1] {ECO:0000313|RefSeq:XP_012868569.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012868569.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_012868569.1; XM_013013115.1.
DR   STRING; 10020.ENSDORP00000004535; -.
DR   GeneID; 105983277; -.
DR   KEGG; dord:105983277; -.
DR   CTD; 4628; -.
DR   InParanoid; A0A1S3EX94; -.
DR   OrthoDB; 2877572at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF24; MYOSIN-10; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
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|ARBA:ARBA00023054};
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}; Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT   DOMAIN          31..81
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          85..793
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          671..693
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1137..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1707..1728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1884..1986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1707..1727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1884..1925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1960..1975
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         188..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1986 AA;  230267 MW;  CA5B9AD367AEB277 CRC64;
     MAQRTGVEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVLV
     ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTCQFL
     LMPELCYHMY TDVELFIILV NHVKRASISV MPPTKLTKLT SNHNPLYRKT SNRNPLYHRE
     DQSILCTGES GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PGELERQLLQ ANPILESFGN
     AKTVKNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG
     AGEHLKSDLL LEGFSNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV
     SSVLQFGNIS FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK
     AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS
     FEQLCINYTN EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG
     VLALLDEECW FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE
     WLMKNMDPLN DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF
     RTVGQLYKES LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI
     CRQGFPNRIV FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF
     RAGVLAHLEE ERDLKITDII IFFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR
     HWQWWRVFTK VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN
     ILAEQLQAET ELFVEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA
     HIQDLEEQLD EEEGARQKLQ LEKVTAEAKI KKMEEEILLL EDQNSKFIKE KKLMEDRIAE
     CSSQLAEEEE KAKNLAKIRN KQEVMISDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ
     IAELQAQIDE LKIQLAKKEE ELQGALARGD DETLHKNNAL KVVRELQAQI AELQEDFESE
     KASRNKAEKQ KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKNH
     EAQIQDMRQR HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES
     EHKRKKLDAQ VQELHAKVSE GDRLRVELAE KANKLQNELD NVSTLLEEAE KKGIKFAKDA
     SSLESQLQDT QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE QQEEEEEARK NLEKQVLVLQ
     SQLAETKKKV DDDLGTIESL EEAKKKLLKD VEALSQRLEE KALAYDKLEK TKNRLQQELD
     DLTVDLDHQR QIVSNLEKKQ KKFDQLLAEE KNISARYAEE RDRAEAEARE KETKALSLAR
     ALEEALEAKE EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE
     LEDELQATED AKLRLEVNMQ AMKAQFERDL QTRDEQKEEK KRLLIKQVRE LEAELEDERK
     QRALAVAAKK KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE
     IFAQSKESEK KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEIANS ASGKSALLDE
     KRRLEARIAQ LEEELEEEQS NMELLNDRFR KTTLQVDTLN TELAAERSAA QKSDNARQQL
     ERQNKELKAK LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK
     LKEIFMQVED ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA
     TEANEGLSRE VSTLKNRLRR GGPISFSSSR SGRRQLHIEG ASLELSDDDT ESKTSDVNEA
     QPPQSE
//
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