ID A0A1S3U5W9_VIGRR Unreviewed; 1081 AA.
AC A0A1S3U5W9;
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=Kinesin-like protein KIN-7D, mitochondrial {ECO:0000313|RefSeq:XP_014501420.1};
GN Name=LOC106762180 {ECO:0000313|RefSeq:XP_014501420.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014501420.1};
RN [1] {ECO:0000313|RefSeq:XP_014501420.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014501420.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR RefSeq; XP_014501420.1; XM_014645934.2.
DR AlphaFoldDB; A0A1S3U5W9; -.
DR STRING; 3916.A0A1S3U5W9; -.
DR GeneID; 106762180; -.
DR KEGG; vra:106762180; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000087766; Chromosome 5.
DR GO; GO:0005874; C:microtubule; 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; cd01374; KISc_CENP_E; 1.
DR CDD; cd16649; mRING-HC-C3HC5_CGRF1-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF35; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 99..416
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1035..1070
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..500
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 644..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 708..784
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 813..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 891..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1081 AA; 119854 MW; D25DD44B66E2F09D CRC64;
MASSSRGRSS SPFSYRKPST PYSSTSSSSS FTNGRLMPRS GSSSTSSFFN SGGRSMTPSR
GRTESTYNGS RGYAGRSPVA FGEEDLIAEP VDSSKSGDSI SVTIRFRPLS EREYQRGDEI
AWYADGEKIV RNEYNPATAY AFDRVFGPHT NSDEVYEVAA KPVVKAAMEG VNGTVFAYGV
TSSGKTHTMH GDHNSPGIIP LAIKDVFSMI QDTPGREFLL RVSYLEIYNE VINDLLDPTG
QNLRVREDAQ GTYVEGIKEE VVLSPGHALS FIAAGEEHRH VGSNNFNLFS SRSHTIFTLM
IESSAHGDDY DGVIFSQLNL IDLAGSESSK TETTGLRRKE GSYINKSLLT LGTVIGKLSE
GKASHVPYRD SKLTRLLQSS LSGHGHVSLI CTVTPASSNM EETHNTLKFA SRAKRVEIYA
SRNKIIDEKS LIKKYQREIS VLKLELDQLK KGMLVGVNHE EILTLKQKLE EGQVKMQSRL
EEEEEAKAAL MSRIQRLTKL ILVSSKNAIP GYLTDVPNHQ RSHSVGEDDK LDALPDGVLI
ENESQKDTSA VSSDLFHDGR HKRSSSRWNE EFSPASSTIT ESTHAGELIS RTKLTMGGMT
ASDQKDLLVE QVKMLAGDVA LSTSTLKRLM EQSVNDPEGS KIQIENLERE IQEKRKQMKV
LEQRLIEIET GDSPVSNSSL IEMQQTVTRL MTQCNEKAFE LELKSADNRV LQEQLNDKCS
ENRELQEKVK QLEQQLATAT SGTLLTSSEQ CASGEHADEL KKKIQSQEIE NEKLKLEQVH
LSEENSGLRV QNQKLSEEAS YAKELASAAA VELKNLAGEV TKLSLQNAKL EKELMATRDL
VNSRGAVVQT VNGINRKFGD ARSGRKGRIS SRANEISGAV VDDFESWSLD ADDLKMELQA
RKQREAALEA ALAEKEFVEE QCRKKAEEAK KREEALENDL ANMWILVAKL KKEGDAVPES
NMDKKNDGAQ QLNGTKINDI ESNTVPKEQL FDAPKPDDEI PKEEPLVVRL KARMQEMKEK
ELKYLGNGDA NSHVCKVCFE SPTAAILLPC RHFCLCKSCS LACSECPICR RNITDRIFAF
T
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