SMC5_CHICK
ID SMC5_CHICK Reviewed; 1065 AA.
AC Q5ZJY5; Q5F3U6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE Short=SMC protein 5;
DE Short=SMC-5;
GN Name=SMC5; Synonyms=SMC5L1; ORFNames=RCJMB04_14g12, RCJMB04_6o14;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved
CC in repair of DNA double-strand breaks by homologous recombination. The
CC complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The
CC complex is required for telomere maintenance via recombination and
CC mediates sumoylation of shelterin complex (telosome) components.
CC Required for recruitment of telomeres to PML nuclear bodies. Required
CC for sister chromatid cohesion during prometaphase and mitotic
CC progression; the function seems to be independent of SMC6 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC6. Component of the SMC5-SMC6
CC complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1 and
CC NSMCE4A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Chromosome, telomere {ECO:0000250}. Note=Associates with chromatin.
CC {ECO:0000250}.
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC6, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
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DR EMBL; AJ720299; CAG31958.1; -; mRNA.
DR EMBL; AJ851554; CAH65188.1; -; mRNA.
DR AlphaFoldDB; Q5ZJY5; -.
DR SMR; Q5ZJY5; -.
DR BioGRID; 688950; 1.
DR STRING; 9031.ENSGALP00000024348; -.
DR PaxDb; Q5ZJY5; -.
DR PRIDE; Q5ZJY5; -.
DR VEuPathDB; HostDB:geneid_431608; -.
DR eggNOG; KOG0979; Eukaryota.
DR InParanoid; Q5ZJY5; -.
DR PhylomeDB; Q5ZJY5; -.
DR PRO; PR:Q5ZJY5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA damage; DNA recombination; DNA repair; Mitosis; Nucleotide-binding;
KW Nucleus; Reference proteome; Telomere.
FT CHAIN 1..1065
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000270953"
FT REGION 441..627
FT /note="Flexible hinge"
FT COILED 134..156
FT /evidence="ECO:0000255"
FT COILED 186..400
FT /evidence="ECO:0000255"
FT COILED 628..805
FT /evidence="ECO:0000255"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 27
FT /note="S -> F (in Ref. 1; CAH65188)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> A (in Ref. 1; CAH65188)"
FT /evidence="ECO:0000305"
FT CONFLICT 404..408
FT /note="TTEKI -> HREN (in Ref. 1; CAH65188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1065 AA; 124924 MW; 32F6A0BA2691077B CRC64;
MAVQTRLRAE GSQLRLCDTH HAGKPRSVEG SIVRIYMENF LTYDICEVRP GPNLNMIIGA
NGTGKSSIVC AICLGLAGKP SFLGRAEKVG LFVKQGCLKG LVEIELFKVP ENIIITREIQ
VVTNTSTWHI NRKLTTLKTV EEQVAALNIQ VDNLCQFLPQ DKVGEFARMS KIELLEATEK
SIGPPEMYQF HCKLKSLKEK ERELENVCKD KVNSLEKMKQ RAERYKQDVD RYHECKRHLD
LIDMLQRKRP WVEYETVRQQ HEDVKQRRDQ AKEELKNLKE MQSPLTKKIR ECEEFYNSLN
MKIKNTADEI KGVSQKCKEK QDALEMKDKQ ISEINQALRM KKDEEVDRKK KILSAYKMID
EWNNELNTVT DCENLQPQID AVNNELKHVQ EERANIDSDI GDVTTEKINQ ERENGRIIDR
IGQLNNIIKV KEETLQARFR DTHSALMWLR KNKHKFKKEV CEPMMLTINV KDNKHAKYVE
NHISTNDMKA FVFESQEDME LFLVELRDRQ KLRVNAVCAP DKSCAETLPS TPIEELHRYG
FFSYLRELFD APLPVMSYLC SQYHVHEVPV GTEKTRNMIE RVIKETKLKQ IYTAEEKYTI
KVSTYTKLSF STNMCLRPAQ FLNYYVDTDE RRQLENQQQN IKHILQSLDK QLMTLCERQK
HLECRDNELR QQKKELLERG SRRKQLESKI AVKYDSIRQL EQNPINLEKE SQQAKVKIRA
INIQKAKLVT ELMCHIKNYV SLNICKADLI LQSTAVDAEK NRLEAEYKAA SVELRASEQR
FLELDERKRI LTENCKELLK KARQMCNMNL DQHLPKEFQT AFQTLPDTLE EIDAFLNEER
SRVSCFTGLS ASVVEECSKQ MEEIQKLMES IEENKKELDD YKQSISKIKE RWLNPLKKMI
ESINEKFSGF FSSMESVGEV DLHVENEEEY DKYGIRIRVK FHNFTDLHEL TPYHQSGGEK
SVSTVLYLMA LQELNRCPFR VVDEINQGMD PVNERRVFEM FVKTACKEST SQYFLITPKL
LQNLTYNEKM TLLFVYNGPF MLEANKWNLK SFCRRRRRLG RMDEQ
