ID A0A1L8EMK6_XENLA Unreviewed; 1943 AA.
AC A0A1L8EMK6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Myosin-7B {ECO:0000313|RefSeq:XP_018093911.1};
GN Name=myh7b.S {ECO:0000313|RefSeq:XP_018093911.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018093911.1};
RN [1] {ECO:0000313|RefSeq:XP_018093911.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018093911.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018093911.1};
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_018093911.1; XM_018238422.2.
DR STRING; 8355.A0A1L8EMK6; -.
DR PaxDb; 8355-A0A1L8EMK6; -.
DR GeneID; 108702765; -.
DR KEGG; xla:108702765; -.
DR AGR; Xenbase:XB-GENE-11536246; -.
DR CTD; 108702765; -.
DR OMA; ITMLQAF; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 108702765; Expressed in heart and 4 other cell types or tissues.
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 CDD; cd14927; MYSc_Myh7b; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 3.
DR Gene3D; 1.20.5.370; -; 5.
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 Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 2.
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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF29; MYOSIN-7B; 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; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 5.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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}; Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT REGION 664..686
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1913..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 851..1165
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1943 AA; 223955 MW; 4A140813EA8AE2AF CRC64;
MSSLLDMTEF GEAADYLRKS DRELMKLQTI PFDGKKKAWI PDDKEAYIEV EIKDSSGGNV
NVETKDKKTL SVKEDDIQQM NPPKFDMIED MAMLTHLNEA SVLDNLKRRY ANWMIYTYSG
LFCVTVNPYK WLPVYTATVV AAYKGKRRSE APPHIYSIAD NAYNDMVRNR ENQSMLITGE
SGAGKTVNTK RVIQYFAIVA ALGEGFGKKS QAPATKTGGT LEDQIIEANP AMEAFGNAKT
LRNDNSSRFG KFIRIHFGPT GKLASADIDI YLLEKSRVIF QQPGERSYHI YYQILSGKKP
ELQDMLLVST NPYDYHVCSQ GVTTVDNLDD GEELMATDHA MDILGFSQEE KTGSYKIVGA
VMQFGNMKFK QKQREEQAEA DGTESADKAA YLMGISSADL IKGLLHPRVK VGNEYVTKGQ
NVEQVVYAVG ALAKATYDRM FKWLVSRINK TLDTKLARQF FIGVLDIAGF EIFEYNSFEQ
LCINFTNEKL QQFFNHHMFV LEQEEYKKEG IEWVFIDFGL DLQPCIDLIE KPMGILSILE
EECMFPKASD MSFKAKLYDN HLGKSPNFQK PKLDKKRRYE PHFELMHYAG VVPYNIMGWL
DKNKDPLNET VVTVFQKSSN KLLASLYENY ISSYSVEHQK PGVKEKRKKA ASFQTVSQLH
KENLNKLMTN LRSTQPHFVR CIIPNESKTP GVMDPFMVLH QLRCNGVLEG IRICRKGYPN
RLLYADFKQR YRILNPNAIP DDKFVDSRKA TEKLLGSLDI DHTQYKFGHT KVFFKAGLLG
QLEEMRDERL AKIITMLQAR SRGRLMRIEY HKIIARRYAL MVIQWNIRAF NAVKHWSWMK
LFFKIKPLLK SAQTEKEMAN MKEEFLKLKE ALEKSEAKRK ELEEKQVTLI QEKNDLGLQL
QAEQDNLADA EERCDLLIKT KIQLEAKVKE LTERLEDEEE MNSDLTSKKR KLEDECAELK
KDIDDLEITL AKVEKEKHAT ENKVKNLIEE MAALDEIIAR LTKEKKALQE AHQQALDDLQ
AEEDKVNTLT KAKAKLEQQV DDLEGSLEQE KKLRMDLERS KRKLEGDLKL TQESVMDLEN
DKQQLEEKLK KKDFETSQLN SRIEDEQMMC AQLQKKIKEL QARIEELEEE LEAERATRAK
VEKQRAEVAK ELEELSERLE EAGGATSVQI EMNKKREAEF LKLRRDLEEA TLHHEATAAG
LRKKHADTVA ELGEQIDSLQ RVKQKLEKEK SEMKMELDDF TSNIEQLTKN KANAEKLCRT
FEDQLSEAKC KVDELQRQLA DISLHRARLQ TENGELSRLL EEKESFVNQL SRGKASFTQS
IEELKRQLEE ETKAKNALAH ALQASRHDCD LMREQYEEEQ EAKGELQRSL SKANAEVAQW
RNKYETDAIQ RTEELEEAKK KLAARLQDAE QAVETANAKC SSLEKTKHRL QTEIEDLVID
LERANSAAAA LDKKQRNFDR ILGEWKQKYE ETQAELEASQ KESRSLSTEL FKLKNAYEES
LDNLETMKRE NKNLQEEIAD LTDQISASGK MIHELEKVKK ALESEKSDIQ AALEEAEGAL
EHEESKTLRI QLELSQIKAD VDRKVAEKDE EIENLRRNHQ RAMESMQASL DAEAKARNEA
IRLKKKMEGD LNEMEIQLNH ANRQAAESQK MVRNLQSHVK DLQIELDDTL RHNDDLKEQA
AALERRNSLL LAEVEELRAA LEQAERGRKL AEQELLEATE RVNLLHSQNT GLINQKKKLD
ADISQLTTEV EESVQECSNA EEKAKKAITD AAMMAEELKK EQDTTAHLER MKKNMDQTIK
DLQMRLDEAE QIALKGGKKQ IQKLEAKVRE MEGELENEQK KNAETQKGIR KYERRIKELT
YQTEEDRKNL ARMQDLIDKL QMKVKSYKRQ SEEAETQANS NLLKYRKIQH ELDDAEERAD
VAEGQVNKLR ARTREAASSK HEE
//