ID A0A154P6T7_DUFNO Unreviewed; 2090 AA.
AC A0A154P6T7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Centromere-associated protein E {ECO:0000313|EMBL:KZC07054.1};
GN ORFNames=WN55_08938 {ECO:0000313|EMBL:KZC07054.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC07054.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC07054.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC07054.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC07054.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; KQ434820; KZC07054.1; -; Genomic_DNA.
DR STRING; 178035.A0A154P6T7; -.
DR EnsemblMetazoa; XM_015572975.1; XP_015428461.1; LOC107185315.
DR Proteomes; UP000076502; Unassembled WGS sequence.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
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 Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000076502}.
FT DOMAIN 4..321
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 500..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2068..2090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 599..640
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 781..850
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1006..1033
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1062..1138
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1188..1240
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1267..1332
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1440..1467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1525..1594
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1623..1840
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1900..1934
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2090 AA; 241566 MW; 10801ED515F58B42 CRC64;
MSESVKVGIK VRPLIECEKN KNLPIQWIVQ GNSIVSLDPE TIKRGDSEFH FDYIFDLDAT
SSNVFDSIVK PIVIATVNGF NGTVFSYGQC SSGKTHTMIG NSGELGIIPL SIMYMFKTIS
NTIEREFLLR VSYLEVQNET INDLLNKDGI ELKFHKDNEH ATVDCKEEIA NTSDKMLSIM
KKGIKIRKTR ETDRNDSISG HSIFRITIES REISGESKSI VQVSQLNLVD LAGFESAREI
AGIQEPQQTD KSLSMFESII VQLSQSQNEQ RDINVRHSKL TELLQSSLGG NSLTAIICTI
IPVASKETYF TLSFARQAKN VKNKPRKNKV SSDAPFLIRY SEQLTKLQTE LQRIKNGKSP
IEVGSIEPKW QENYQINHLL EERVRLLKTQ IISGCNANYA EPVKCKSRRR QSWCNPGTFK
SHLPVFQTKT GLPTIKEMSP EKPQRKSNMQ SIAVTNQTFQ TGFTDFELDL IECNEGSEVK
ENGISLGEME FTNNVLTEET EGNNSCMTPE KQDSSVQTSS NQGSPSTPKN VLRKYICDLT
QDLIELREFT TLEKQLMCGE ATLYDVISIS KNLDEHTAEE SASSSFKQNE LFEYSSNVAI
QLEEEKVKLA EELELKIQEL DEIKNDIQGF KLDVEKLQNT IFLLTNENME MSTKLTAEKE
RSKQIEFNLQ RTIDELYARI SKVTDEKISL ESDVMVLNDQ LQSLRLKTLE VYSDEQMLVK
YQNKIDALKT ENIESTAIIA EKNKELESIK ESKSLLYDHE CIYKDKTALL TEEKASLVLE
NNELSTDLID KIEENDMLRE ECDILKNKIS ITEQHVNADE NDVEQLRSEN KLLKAEIMEL
KIKVTMLSDE NVRFSNNLLE TMEDLDHSRN EKLANNSLHS SSVFDNTIKK NKSAKEILLE
NNNETLADKV TMLQDKVDHL TRLNKKLSEL KLSSCSQCVH LKSLNDSRRV LKLEAKALNC
KLYELQKKFD QKCADTEALK QKANQELNLS FVDASLNASF ADGLNVSFVE EKVQHLHNEL
QILKDDREKL SVMYREKCDE LEKLHDEVGE STNVDSKSKK HVVKHESRIQ QIQQSIDQVR
DDIDELKKNS TNFTSVFNKF RTEKASLLDE INALRHMNEK LQQKVSDTEI SAATATEKAH
ILETELLSMS KEIEEYTLKE KVIRGEKLTL EVELEDLKAE KENKDICITA LHKTIDDLNE
CISSLKNELD LMTKESENDK EILKQQLQTL EVQLTDSKDN LAVKYKTEFE SITRKFEEYT
KESEIKLKKI NETLNKYVDE NDNLTQELAK LRDIELKFQD MKEKNEHVFI EEKTLANENE
KLKEELNTVR ECMMKELKSF KSKVNSVDYL SKTANEIFII FLQTLMSKEE EVIKTMRELF
EKDKQKLVDE KRQSADAKKR VTSWAKELEM ETEKLQMDLT KRETMYKQQQ DKIYHLEYVL
RDANYEKETL KEKVETLEVD FNNLQAEFDK QSKVDIRQEE AISVAQKREK AVQEDFKKRE
IELQFKVRSE KEIYEKRIDE LVYAIESYKT KNMELKGNIE GLEVNEKQLK NIIEANASEL
KANSQTIHKL NIELEQLTEA YNEVNHEVEQ KTSHIEEIKA LLKSKCDKIS EYKAKLDTVV
PDYEILKDQV KERKANIERY KEEIGELKME KEKQIAMIKD NLNSEEIKNV GLNKQLHELN
NKNIALAEEL DTLKEKYEEL QHANAKLERK IRNSTSKVKA EADMEDLRDV NKRLQNNLEG
ASNRITELQD SKNKILKELV NLKGQYELLS QENMEIKKTL ASYKSRQSIP NSSQDDGRYD
ALLQEKNKIA LELEDKKLLL KQKEKEVREH VSRVQDLTVK NKEFDEYLRD HATVIREREA
EISQLKDKLY VHQIENKLVH ENKIFNEKRQ IENLTCEIDV DESDEICQML RKKIQELELQ
IVSKNGQIAT LEIQIQSENF PYQQKCKELE EHLCYSFIFD RMQNFVLKKW RTNRRDQYCQ
TSPNNASQLF TLNNEVGSVP SREVEKAEGK FWTHWNKDTK QFFLQFAFKN EKPSVGKVPP
PPVPLIRPGL GPPMVPVPPP PRPPMFNPVP PPPALLATGM QIPPPPPHLA
//
