ID A0A452I1G0_9SAUR Unreviewed; 1700 AA.
AC A0A452I1G0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000021299.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000021299.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000021299.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR Ensembl; ENSGAGT00000024255.1; ENSGAGP00000021299.1; ENSGAGG00000015625.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22726; FHA_KIF1A; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR049779; FHA_KIF1A.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 525..581
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1585..1683
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1415..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 637..686
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1415..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1700 AA; 192332 MW; 2BC552EB0F50B956 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM TGSTTTIVNP KQPKETPKSF SFDFSYWSHT
TPEDINYASQ KQVYQDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGR QEKDQQGIIP
QLCEDLFSRI NDATNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETDITTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAVI
NEDPNNKLIR ELKDEVARLR DLLYSQGLGD IIDTNTAPGR PKLTNALVGM SPSSSLSALS
SRAASVSSLH ERIMFAPGSE EAIERLKETE KIIAELNETW EEKLRRTEAI RMEREALLAE
MGVAMREDGG TLGVFSPKKT PHLVNLNEDP LMSECLLYYI KDGITRVGRE DAERRQDIVL
SGHFIKEEHC IFRSNTKASG EVVVTLEPCE GADTYVNGKK VMEPSVLRSG NRIIMGKSHV
FRFNHPEQAR QERERTPCAE TPAEPVDWAF AQRELLEKQG IDMKQEMEQR LQELEDQYRK
EREEANYLLE QQRLDYESKL EALQKQMDSR YYPEANEEEE EPEDEVQWTE REFELALWAF
RKWKWYQFTS LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPNA
AKDREKRPFP RTIVAVEVQD QKNGATHYWT LEKLRQRLDL MREMYDRAAE VPSSILEDCD
NVVTGGDPFY DRFPWFRLVG RAFVYLSNLL YPVPLVHRVA IVSEKGEVKG FLRVAVQAIS
ADEEAPDYGS GVRQSGTAKI SFDDQHFEKF QSEACPMAGM SRSGTSQEEL RIVEGQGQIT
DIGPSADEVN NNTCGVTPDD LLLDSPEKVA LDDPLEAVLD HLTLGSIFTF RVTVLQASSI
SAEYADIFCQ FNFIHRHDEA FSTEPLKNTG RGPPLGFYHV QNIAVEVTKS FIEYIKSQPI
VFEVFGHYQQ HPFPPLCKDV LSSLRPSRRH FPRVVPLSKP VPATKLSTLA RPSAGPCQCK
YDLMVFFEIC ELEANGDYIP AIVDHRGGMP CLGTFLLHQG IQRRITVTLV HENSSLVRWK
EVRELVVGRI RNTPEGDESL IDPNILSLNI LSSGYVNPSQ DDRTFYQFEA AWDSSMHNSL
LLNRVTPYRE KIFITLSAYI EMENCTQPAV ITKDFCMVFY SRDAKLPASR SIRNLFGSGS
LRASESNRVT GVYELSLCRV ADAGSPGMQR RRRRVLDTSV AYVRGEENLA GWRPRSDSLI
LDHQWELEKL SLLQEVEKTR HYLLLREKLE TTQRSGLESL SPCSSEDSES HSTSCVSSPL
SADGASEGRS SPLETPSERQ KELAVKCLRL LTHTFNREYS HSHVCISASE SKLSEMSVTL
QRDPSMTALG VTTLTPSSTC PSLLEGRYNA TEVRTLHLSS RAESPEPEPI AEGEQKKSPT
HGPEDEKETQ RLLVPDIQEI RVSPIVSKKG YLHFLEPHTN GWVKRYVVVR RPYVYIYNTD
KDSVERAILN LSSAQVEYSE DQQAMLKTPN TFAVCTEHRG ILLQASSDKD MHDWLYAFNP
LLAGSIRSKL SRRRTAQMRI
//