ID A0A3B4DXM6_PYGNA Unreviewed; 1217 AA.
AC A0A3B4DXM6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000027749.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000027749.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement. {ECO:0000256|ARBA:ARBA00034085}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000256|ARBA:ARBA00004584}. Nucleus
CC {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR RefSeq; XP_017541770.1; XM_017686281.1.
DR AlphaFoldDB; A0A3B4DXM6; -.
DR STRING; 42514.ENSPNAP00000027749; -.
DR Ensembl; ENSPNAT00000001752.1; ENSPNAP00000027749.1; ENSPNAG00000007202.1.
DR GeneID; 108413659; -.
DR CTD; 9126; -.
DR GeneTree; ENSGT00580000081628; -.
DR OMA; DQHQSMR; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719}.
FT DOMAIN 530..643
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..503
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 675..853
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 962..989
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1217 AA; 141515 MW; 6E0A8E5CADE408BB CRC64;
MYIKQVIIQG FRSYRDQTVV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK
ETEGKREKIN ELLKYIEERL HTLEDEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD
ELSSKRETCG DKSRQLRDAQ QDARDKVEET ERVVRELKAR ISAMKEEKEQ LSAERQEQIK
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELQETEPK FNTVKEKEER
GISRLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL
EDTEANKEKN LEQYNKLDQD LNEVKTRVEE LDKKYYEVKN RKDELQSERN YLWREENAEQ
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLEHFR RKGINQHVIN GYHGIVMNNF
ECEPAFYTCV EVTAGTRLFY HIVETDEVST KILMEFNKMN LPGEVTFLPL SKLDVRDTAY
PETNDAIPMI SKLRYSPNFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH
RGALTGGYYD TRKSRLELQK DMRKAEEELA ELEAKLNENL RRNIERINNE IDQLMNQMQQ
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLLSQLS LEDQRRVDDL NDEIRQLQQD NRQLLNERIK LEGIMTRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSELDGIN KRIKDTMARS EDLDSLIDKT EIEIKDHIKS
MDRWKTIEKE QNDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
TLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQDELDRG YKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DAEGGQSQDE GEGGTDSERG
SASQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY
LFDEIDQALD AQHRKAVSDM IVELAGHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV
ISAEQAKDFV EDDTTHG
//