ID A0A0M8ZY39_9HYME Unreviewed; 1953 AA.
AC A0A0M8ZY39;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cytoskeleton-associated protein 5 {ECO:0000313|EMBL:KOX71953.1};
GN ORFNames=WN51_03230 {ECO:0000313|EMBL:KOX71953.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX71953.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX71953.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX71953.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX71953.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC {ECO:0000256|ARBA:ARBA00025722}.
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DR EMBL; KQ435827; KOX71953.1; -; Genomic_DNA.
DR STRING; 166423.A0A0M8ZY39; -.
DR OrthoDB; 5477703at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0099080; C:supramolecular complex; IEA:UniProt.
DR GO; GO:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 3.
DR SMART; SM01349; TOG; 5.
DR SUPFAM; SSF48371; ARM repeat; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 1..227
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 269..506
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 572..803
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 839..1054
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1118..1346
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 518..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1953 AA; 218866 MW; 73D3BD11B3AC631C CRC64;
MEQDTEYVKL PLEERCVHKL WRARLHGYKE CVNTFQCIDD EKSPEWNKFL GFIKKFVVDS
NAVAQEKGLE AALAFVENAA VAGKTVGEVM NGIVTKCIAA PKAKTKELAV QITLMYIEIE
KHEAVQEELL RGTEAKNPKI VAACISILTL ALRQFGPKVI NIKSLIKKIP GFLEDRDKTV
REEGKFMVVE IYRWIGAPLK QQLNTLKPVQ ITELEAEFNN LKEEKVVPTR FLKSQKTKVI
CITDSTSDIG EEGKDDGDSV FAPDVDPYEL LEPVDILSKL PKDFYEKIEA KKWQERKEAL
EALDSLVKNP KLENGDYGDV VRALKKIISK DTNVLVVALA GKCLAGLAFG LKKRFQPYAT
ACLSSILEKF REKKQNVVQA LREAADAIFL SVSIDLILDD TLAALENKNP AVKAETATYL
ARCFSRTPPL TLNKKLLKAY TSVLLKTLNE SDPTVRDSSA EALGTAMKLI GEKSMMPFLT
DIDNLKMTKI KECAEKAVIH VNVPSTLKVI VERPNTAPSK IESTAKGKEP EPKARRPNTA
KKLPSKKPSA SSLTNLAGSK KSTSTKIQAE KNYSIEEIEE MAIQMLPNDI LSGLVDSNWK
TRLAAVEQLL EFVKQIDPTE IPIQVIVRTL AKKPGFKDTN FQVLKLRLEI VKFLAENYPF
STTVCEYCIM DITEKLGDTK NSAVAGETLL VIAEATSLEY VAQEIIAFAF NQKNPKVQQE
TLALLCRGLV EFGYVINIKS LMENIKKAVT ATNPGVRTSA IALLGTLYLF MGKPLLMFFE
NEKPALRQQI EQECEKHNGE SPPVPIRGIK NKKDKTSDDD EDIEIDKKST SNSDPDINNL
IPRVDISNQI TEGLLNELSD KNWKVRNEGL QKVNAIISEA KFIKGSIGDL PQALALRLID
SNSKIAQSTL GICQILAVAM GPPAKQHIRV LFPGFIQCLG DNKNWIRTAA ISCINTWGDQ
CGYKEFFDGE MIGDALKSGS PILRAEVWSW LAQKLSLIPT KQIPKEELLK LKPGSRTVVL
AALDKSRPNL PMKPLPKKQS LKENNQKVVK SAGALKAAKA VVKPNQKQPT SKPGSARKKD
DDVDTSPLLA TNNLKHQRVI DEQKLIVMKW NFTTPREEFV ELLKELMTAA NVNKTLLANM
FHSDFRYHLK AIEALIEDLP DNSKALVSNL DLILKWLTLR FFDTNPSVLL KGLEYLRMVF
NLLIENQYHM LENEAASFIP YLIIKIGDPK DAVRNGVRAL FKQIALVYPV SKLFSYVMEG
LKSKNARQRT ECLDQLGSLI ENYGLSVCQP STSVALKEIA KQIADRDNSA YFLQGERIYK
LIGQISEKDQ SLLDERIKRA SKNYPTKSAS TNRLSVASNA TPISSTSSNE DVKTSNEEYE
EESDDTPEPQ PPVSSQTNEL THLIETTNVT TETNEINEPL SNTPQEINIS SPRYEDDIKT
NSPVLAQPKV SGPFGLDMDF LQKIELNAPV KYSNPVLVEI DLTDLNENPN TNIHEVPVIP
MSPPKLLVSK SATMTQQQLS AANTSKEDSL ERKILAMSSL DLAVAIQSMN SIDNLIKSHQ
ILSLQSKEDK FIGSINMQLK LLQTYPLQQG GADISKGFRN TFMVLLAFYD TGILGKNVPL
IHLKELVDQM ISLLAENKLN HLQQADAYYR VINNITIQII LLSYGNNYKN LIFIENIKTL
NRANSLIPLM FPCSVLIKLL HGCAESTAPS KYEELVMKCL WKIVKTIPNW AADLDYDTIL
LEVHRFLKDY PSVWWKKRKS DTPLRTIKTI LHSMTRVKGS TILSHLTRIN NTNESELQSY
LIRLIATFKP DEMNSNPKTS LKTSSAGKTQ EHLSKFTHQQ LSEIFKKIGS KEHTKEGLTQ
LYDFKLQYPE ADVQPFLVKS HQFFQDFIEQ GLRDIDQARK NQNLITQTNN QYSTEIAESA
SSEEKSLMDP LHRLEKLRAS EAQCRTTSQS SPT
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