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Database: UniProt
Entry: A0A3B5A3M1_9TELE
LinkDB: A0A3B5A3M1_9TELE
Original site: A0A3B5A3M1_9TELE 
ID   A0A3B5A3M1_9TELE        Unreviewed;      1642 AA.
AC   A0A3B5A3M1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Kinesin family member 21B {ECO:0000313|Ensembl:ENSSPAP00000015848.1};
GN   Name=KIF21B {ECO:0000313|Ensembl:ENSSPAP00000015848.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000015848.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000015848.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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; ENSSPAT00000016103.1; ENSSPAP00000015848.1; ENSSPAG00000011855.1.
DR   GeneTree; ENSGT00940000159650; -.
DR   Proteomes; UP000261400; Unplaced.
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   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01372; KISc_KIF4; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 6.10.250.2730; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF34; KINESIN-LIKE PROTEIN KIF21B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          8..375
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REPEAT          1326..1365
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1366..1399
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1522..1561
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1563..1604
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1605..1634
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          501..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1261..1283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          665..847
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          978..1043
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        504..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..652
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1642 AA;  183584 MW;  1ADFE5DF444E5641 CRC64;
     MASQGDCCVK VALRIRPQMA KEKIEGCHVC TLVTPGEPQV LLGKDKAFTY DFVFDIDSEQ
     QHIYQACVYK LIEGCFEGYN ATVFAYGQTG SGKTYTMGTG FDVSLTQQEQ GIIPRAVHQL
     FEGIQNRRLR AQETGSQPPE FKVSAQFLEL YNEEILDLFD GARDPESRSR KSNIKIHEDA
     SGSIYTTGVT SRLVHTEEEL LQCLKLGALS RTTASTQMNA QSSRSHAIFT IHLCQMRVCQ
     QLQMQNGGGE NGELNGVDSN PIAQPEYETL MAKFHFVDLA GSERLKRTGA TGERAREGIS
     INCGLLALGN VISALGDQTK KGGHVPYRDS KLTRLLQDSL GGNSRTVMIA CVSPSDRDFM
     ETLNTLKYAN RARNIKNKVV VNQDKTSQQI SALRAEIARL QMELMEYKAG KRVACEDGSE
     GYSDLYQENA MLQRENDTLR LRVKAMQETI DHLNTRVTHL LANEVSTLLT KSSEGNEEIG
     TLIQNYIREV EELRTKLLES ESMNESLRRQ AARLSARSPF PASSLSPAPG HPPGSSPAPM
     SMEAEMTDVL RRAKLDIERL KKKERRQRRM SPELEKGLKK RVKLHTHENG ENGQSGENGQ
     NGEIDSDDNY TEDIMSPLQE ESGCDEDEGE DEEECREEED EFDSDESLVD SDSDSDEKAN
     FQADLADLTC EIEIKQKLID ELENSQRRLL MLKLQYEEKL ILLQNKIRDT QLERDRVLQN
     LMSMENYTEE KANKIKQEYE KRLKEMNRDL LKLQAAQKEH ARLLKNQGRY ERELKKLQAE
     VNEMKKAKVT LMKQMKEEQQ RRRMVEAKRN REIAQLKKEQ RRQEYQIRAL ESQKRQQEMV
     LRRKTQEVTA LRRLAKPMSD RVAGRVARWN QTPPVTDSGA ELSASTTASS SEPETARTVS
     GLVRQWNNKN SVYGYLGESE GSMDGTRVIG RKKLQRKPLG IGNIGAAGRA SSFSKSARQK
     WQALERRIMD IVMQRMTISN VEADMDRLIK KREELTVQQE ALSHKREVLM AEGEGPEAED
     RLLQEINEDI EVLNANIDYI NDSLSDCQAT IVQIEETKDE LDSVDTSVVI SSCSLAEARH
     LLDHFLKASI DKSLQVAQKE TQIRLLEGQL RQTDVIGSSH NHIILDALRE KAEYIPELQA
     LIHNVQQENG YASTDEEPSE FSQASDSSVS QMKESNSQED FKLKIEPRLS AQMKAVSAEY
     LGPILDPTSG SKPQHITKSL ASLTDIQEDG LSLVTGSLGL SLALRDPYHR DRASRTISLP
     VRGHTLPTDG YTPPSSPPLR TRNDRNVFSR LTSNQTQGSA LDKGVINPIG GVKGGRTAPL
     QCVSVAEGHS KPVLCVDATD ELLFTGSKDR TCKMWNLVTG QEIVTLKGHP NNVVSVKYCP
     SSCLVFSVST SYIKVWDIRD SAKCIRTLTS SGQVVSGDAC AGTTTRTITF AQGECQINQI
     AINPSGSVLY AAAGNTVRMW DLNRMQAMGK LTGHIGSVMC LTVGQSLLGK DQVITGSKDH
     YVKVFDVAEG TMGNVGPAHN FEPPHYDGIE CLAVQGDVLF SGSRDNGIKK WELEQQELTQ
     QIPNAHKDWV CALAYVPGRP MLLSGCRGGM LKVWNVENFT PIGEVRGHES PINAICTNSR
     QIFTASSDKT VKIWLSKVWR KR
//
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