ID A0A087R1D4_APTFO Unreviewed; 2674 AA.
AC A0A087R1D4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Unconventional myosin-IXa {ECO:0000313|EMBL:KFM07288.1};
GN ORFNames=AS27_07025 {ECO:0000313|EMBL:KFM07288.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM07288.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM07288.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM07288.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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; KL226042; KFM07288.1; -; Genomic_DNA.
DR STRING; 9233.A0A087R1D4; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd20883; C1_Myosin-IXa; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd17216; RA_Myosin-IXa; 1.
DR CDD; cd04406; RhoGAP_myosin_IXA; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR028558; RA_Myosin-IXa.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; UNCONVENTIONAL MYOSIN-IXA; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000053286};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..113
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 147..1024
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 2100..2149
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 2164..2352
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 906..928
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1323..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2475..2658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2433..2472
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1464..1505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2487..2507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2528..2543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2545..2567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2622..2636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2674 AA; 306291 MW; 8E4489A59B574B1D CRC64;
MSVNDVGGRR RFEDSEYTLH IYPGSIAEGT IYCPITARKT STAAEVIDSL INKLQLEKTK
CYVLAEVKEF GGEEWILNPT DCPVQRMMLW PRMALENRIS GEDYRFLLRE KNLDGSIHYG
SLQSWLRVTE ERRRMVERGF LPQPQQKDYD DLCSLPDLNE KTLLENLRNR FKQEKIYTYV
GSILIVINPF KFLPIYNPKY VKMYDNHQLG KLEPHIYAVA DVAYHAMLQR RKNQCIVISG
ESGSGKTQST NFLIHHLTAL SQKGFASGVE QIILGAGPVL EAFGNAKTAH NNNSSRFGKF
IQVNYQETGT VRGAYVEKYL LEKSRLVYQE HNERNYHVFY YLLAGASEEE RSAFHLKQPE
EYHYLNQMTK KPLRQSWDDY CYDSEPDCFS VEGEDLKHDF ERLQLAMEMV GFLPKTRRQI
FSLLSAILHL GNIRYKKKTY RDDSIDICNP EILPIVSDLL EVKEEMLFEA LVTRKTVTVG
EKLILPYKLA EAVTVRNSMA KSLYSALFDW IVFRINHALL NSKDMEESTK TLSIGVLDIF
GFEDYENNSF EQFCINFANE RLQHYFNQHI FKLEQEEYRA EGISWHNIDY IDNSGCINLI
SKKPTGLLHL LDEESNFPQA TNQTLLDKFK RQHEGNSYIE FPAVMEPAFI IKHYAGKVKY
GVKDFREKNT DHMRPDIVAL LRSSKNAFIC GMIGIDPVAV FRWAVLRAFF RAMVAFREAG
KRYVEKKTGS GSTWQGHDDA VPCAVLKSVD SFSFLHHPVH QRSLEILQRC KEEKYSITRK
SPRTPLSDLQ GVNTINERTQ RDAYAVGWNG RMGMRHSRLA SPGAFLDKDG IFVNATNSKL
LERAHGILMR NKNFKAKPNL PKHMLDVKSL KHLTNLTLHD RITKSLLHLH KKKKPPSISA
QFQASLNKLM ETLGQAEPYF VKCIRSNAEK LPLRFNDSLV LRQLRYTGML ETVRIRQSGY
SCKYSFQDFV NHFHVLLPQG ISPSKHNIHD FFRKIKLDPD NYQVGKSMVF VKERERQLLQ
DLLHQEVLRR ITLLQRWFRS ILCRRQFLSL RQAAVIIQRF WRRYQSRKQG EPAPDPLVLG
KAAIVLQTHW RGFVERRRFL QMQFAAHLIQ SCWREYAKRR HDAATSIQAA WRGHRAKQSY
TASRSKIVCL QAVCRGYLAR QRFRALKEQR LKEMQLENGL SIREEDGLEA GDALEIKGSD
PSKWEDGSFE ERVRAIEEHI SLMENNRVNH MDPLDTSANL LYKRHERASS QSGMDTEEEV
VVRERPKSLE DLNQKKVVRA KRESRRMREL EQAKFSLELL KVRSTGGLSP SEERRWSTEL
VSEALHSPQG TPESESSQGS FEMLSCEDTP SNKRVSLVLD EQDVQSFSTD SLPSSPQAHL
QEKSFCAADV NSNLPGCRRM PLDSELPDNL TAKERVVCDP QNVIYKAHLR ETFLSSNLPT
FYVPPQENVK VKLVENNLRN KAMEREERTV TFSEVRKDSE PDQGRALGGE EEEKSSTKRE
ERGTATATQA HSPDSVIKRL EKLNVEKEER QKQLQLQNER EMMEQIREQK EILERQRKAF
EQQGRVEALQ RAEQSRMKDP SLKPTKKLDS RPQSVLILHP QSRGEHGPTT GVTPTSSVDI
KGLTVGTRGS SPAHSAPKDR PVSMFMERRE GQSGSALEPR CHSRPALDPR DLPGSHFSRT
ERLRQPRMPN QATEETRASA MFFTPKDNPF GLHREASHQC LSKGELARKP FKMPGSGRGE
VPRPTHKKKA RMARTRSDFL TRGTFADGEG DTEEDDYDGN FEFLLSSDQP PHPEAVPAAR
LGQACYSDSE MTVQRFTSGE GQMKLHKTMS QGEIGKLAAT QKSLAPDGRP QRAKMRFWVK
GKQGEKKTPR EKLATQSELL ELYAEQEAPG REVISGLQLG EELGPHHLTP PRSPELSGIY
RREFKENKEP SPKVKRKRSV KISNVALEPV QWQNDSLQII TSASDLKSMD EFLLKKMNEL
DNEDSKKDTL VDVVFKKALK EFRQNIFSFY SSALAMDDGK SIRYKDLYAL FEQILEKTMR
LEQRDWSESP VKVWVNTFKV FLDEYMIEYK PLDYTAVKVP KTERKKRRKK EVDVVEEHNG
HIFKATQYSI PTYCEYCSSL IWIMDRASVC KLCKYACHKK CCLKTTTKCS KKYDPELSSR
QFGVELSRLT SEERAVPVLV EKLINYIEMH GLYTEGIYRK SGSTNKIKEL RQGLDTDIDN
VNLDDYNIHV IASVFKQWLR DLPNPLMTFE LYEEFLRAMG LQERKETVRG VYSVIDQLSR
THLSTLERLI FHLVRIALQE ETNRMSANAL AIVFAPCILR CPDTTDPLQS VQDISKTTTC
VELIVIEQMN KYKARLKDIN SLEFAENKAK SRLSLIRRSM KPVLIAVRFM SITRSSIPGK
GRVRRGAYPG PTSPVAVRLP SVTDVPEETM SSEEAMEMEV TEQQQAAMQQ EEKVLTEQIE
SLQKEKEELT FEMLTLEPRA SDDETLESEA SIGTADSSEN LNFDSEGAIS DRSERSVALT
SLRPAKAEGP SRLRRHPRTR PDTADPADTS ISSSSSSSPS STSCLPHLPR KRFQMYSKSP
FYRAGGGGEP PETRASPEGF VGPLRYPEDR PQFTTRGTFN PEKGKQKLKS VKTSPPKTKE
PPDGGTGGGR KRNPEADCAA AQPLVLLGSN EFMV
//
