ID A0A093EM52_TAUER Unreviewed; 974 AA.
AC A0A093EM52;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cohesin subunit SA {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=SCC3 homolog {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=Stromal antigen {ECO:0000256|RuleBase:RU369063};
DE Flags: Fragment;
GN ORFNames=N340_08615 {ECO:0000313|EMBL:KFV15606.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV15606.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV15606.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV15606.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the complex is cleaved and
CC dissociates from chromatin, allowing sister chromatids to segregate.
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBUNIT: Part of the cohesin complex which is composed of a heterodimer
CC between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached
CC via their hinge domain, and RAD21 which link them at their heads, and
CC one STAG protein. {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369063}.
CC Chromosome {ECO:0000256|RuleBase:RU369063}. Chromosome, centromere
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000256|ARBA:ARBA00005486,
CC ECO:0000256|RuleBase:RU369063}.
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DR EMBL; KL464710; KFV15606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093EM52; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-UniRule.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:UniProtKB-UniRule.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF2; SCD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11199; STROMAL ANTIGEN; 1.
DR Pfam; PF21581; SCD; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51425; SCD; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU369063};
KW Cell division {ECO:0000256|RuleBase:RU369063};
KW Chromosome {ECO:0000256|RuleBase:RU369063};
KW Chromosome partition {ECO:0000256|RuleBase:RU369063};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|RuleBase:RU369063};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661}.
FT DOMAIN 215..300
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT COILED 179..209
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV15606.1"
FT NON_TER 974
FT /evidence="ECO:0000313|EMBL:KFV15606.1"
SQ SEQUENCE 974 AA; 112637 MW; B4D35429F3F84BFD CRC64;
VEAVTLFEVV SMGKQAMQSV VDDWVEAYKQ DRNVALLDLI NFFIQCSGCQ GMVTAEMFQS
LHKKDVMRKM TETFDEDNED YPLIRTGPYW KKFKANFCEF IAVFVQQCQR SILYDSYLMD
TIISLLTGLA DSMVRAFRHT STLAAMKLMT AVVSVHLNLD VSKHNAQRLY EVEKKRISGK
RTSYRLDQLE RKRKEYEQKL LEIQNMMNAI FKGTFLNRYC DVIPEIRATC AEEIGSWIKT
YPDAFLNDSY LKYMGWMLYD KQAEVRLKCL LGLQGIYSRK ELVSRMDLFT SRFKDRIVSM
PLDKDHEVAV QAMKLLMLMS QNCEDVLSTE DCETLYRFVY TTHRPLAVAA GEFLYKRLLS
HEGDEEVQPK GGGKFGASTD QLKRLICFFL ESELHKHVAY LIDSLWDWAG KFLKDWECMT
TLLLKNAEEG GEALSDAHES TLIEIILATV REAAEGHPPA GRGAAKKILS VKEKKIQLED
CTKITEHFIM VLPQLLAKYS TDAQKVANLL QIPQYYDLDV CSMGHLEKHL DALLREVKDI
VAKHSDVSVL EASSRTYYIL CSEEIAIYNQ VDRARTQLID ELMGQLNQLL DGFWQKEEGF
YEDAGEISRM HSALRRVATF HNAHDLTKWN LYDKTLRLLM FEMKHGSLPV LMILPALQCT
YFSLLWQLAA VSENSPKETL FALRRELRRF SQICMCFLHH KEKDVREKAF MILCDWLLIL
SHQDSNSNEE AVGLLDCLPS TSLQEKLLFF IQEHVFLEEE EESKDLTEEE ERKDESCKLD
DLHKKRSLLA AYCKLIVYNV VEMSAAAEIY KRYVKTYNDF GDIIKETLSR TRHNNKIQSA
KTLILCLQQL FQTHAKSQDS SSGVDFSSAS FTNMKELARR FSLTFGWDQV KSRESVAMIH
KEGIEFAFQR ATGVDGKCLP PNLSFLLIIS EFSNKLLKPD KRLVYTYLQR YVAEPLPCRG
DEWQPLIWYR NSLL
//
