ID   SPDLB_XENLA             Reviewed;         610 AA.
AC   Q6NRW2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Protein Spindly-B {ECO:0000255|HAMAP-Rule:MF_03041};
DE   AltName: Full=Coiled-coil domain-containing protein 99-B {ECO:0000255|HAMAP-Rule:MF_03041};
DE   AltName: Full=Spindle apparatus coiled-coil domain-containing protein 1-B {ECO:0000255|HAMAP-Rule:MF_03041};
GN   Name=spdl1-b; Synonyms=ccdc99-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the localization of dynein and dynactin to the
CC       mitotic kintochore. Dynein is believed to control the initial lateral
CC       interaction between the kinetochore and spindle microtubules and to
CC       facilitate the subsequent formation of end-on kinetochore-microtubule
CC       attachments mediated by the NDC80 complex. {ECO:0000255|HAMAP-
CC       Rule:MF_03041}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000255|HAMAP-Rule:MF_03041}.
CC   -!- SIMILARITY: Belongs to the Spindly family. {ECO:0000255|HAMAP-
CC       Rule:MF_03041}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC070598; AAH70598.1; -; mRNA.
DR   RefSeq; NP_001084803.1; NM_001091334.1.
DR   AlphaFoldDB; Q6NRW2; -.
DR   SMR; Q6NRW2; -.
DR   DNASU; 431843; -.
DR   GeneID; 431843; -.
DR   KEGG; xla:431843; -.
DR   CTD; 431843; -.
DR   Xenbase; XB-GENE-6251766; spdl1.S.
DR   OrthoDB; 1595638at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 431843; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0043515; F:kinetochore binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR   HAMAP; MF_03041; SPDLY; 1.
DR   InterPro; IPR028593; SPDLY_chordates.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW   Kinetochore; Mitosis; Reference proteome.
FT   CHAIN           1..610
FT                   /note="Protein Spindly-B"
FT                   /id="PRO_0000383344"
FT   REGION          474..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..392
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT   COMPBIAS        490..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  70778 MW;  5284274DF048F2A0 CRC64;
     MEESETVLKL RRQLKEAEEE RVKAAHYGLE LLESQSDLQN QLEEQRNEMT GTIENLEQEK
     YSLQREVELK NRMLESLTSE CENIRQQQKL SLEQLEEQLE RNHHRELSEI KDKLEKLKAE
     LDEARLSEKQ LKHKLDYQTE VLANKSEELR MMSERVHETM SSEMLTLQLE KTELETAKDN
     LEQELNELQY REQQLLLTNG NQSRQLERLQ TEKEEREKEA VGYFSALEKA REANQDLQAQ
     LDIALQQAQD PNSKGNSLFA EVEDRRSEME RQLISMKVQF QSLQKQHAFS RQQMHRMKIQ
     IATLLQLKGS HSDPEQLERL QAMVAQKNSE IETLVMKVRQ LEKSQQICEN GPVASSCDGL
     GQGDETYYVD LLKMKLVNSS KEIDKVKDEL SLQRMKALAE SQRVLELERK LFTNDRHLKL
     SQGENMKLRV NLDEMKMKYE PDEMGKIRTQ KRRKEQLPLD CLIDNTSVAV TSGTEAHGVS
     DATPGETCTA ESSDDKKLPK EDLSLSTKDQ DPSSVLLKPN EPPNGQPPKE RKRVRIMEDE
     KDTPDLNKRN PNNCTITSIH PRSTYEESTS ELKKVDEEQE KRKQERKSRL RAPPVLHVPS
     KPATAQCPQQ