ID A0A0L9V3F7_PHAAN Unreviewed; 1268 AA.
AC A0A0L9V3F7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=LR48_Vigan08g010600 {ECO:0000313|EMBL:KOM49279.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM49279.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005231}.
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DR EMBL; CM003378; KOM49279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9V3F7; -.
DR STRING; 3914.A0A0L9V3F7; -.
DR EnsemblPlants; KOM49279; KOM49279; LR48_Vigan08g010600.
DR Gramene; KOM49279; KOM49279; LR48_Vigan08g010600.
DR OMA; HNKIAME; -.
DR Proteomes; UP000053144; Chromosome 8.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 610..730
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 375..402
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 430..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 828..855
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 881..1020
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1074..1118
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1268 AA; 143015 MW; 2B0791F4DB275F3C CRC64;
MQTSRPPDSN LLKLGWEKAR RDAMVMMKVR KQGGKGARLM TSGVLMVMGW CLMVLLRGLL
FLLLEVWIKL QRPHQSKIPK ELIFIIPIQI LCSLHSLPPS TEHAVSRFDL RTLFAMHIKE
VCLEGFKSYA TRTVVSGFDP FFNAITGLNG SGKSNILDSI CFVLGITNLQ QVRASNLQEL
VYKQGQAGIT KATVSIVFDN SDRSRSPLGY EGHPEITVTR QIVVGGRNKY LINGKLAQPS
QVQNLFHSVQ LNVNNPHFLI MQGRITKVLN MKPPEILSML EEAAGTRMYE TKKEAALKTL
EKKQSKVDEI NNLLDQEILP ALEKLRKEKT QYMQWANGNA ELDRLRRFCV AYDYVQAERI
KDNAASEVEG VKGKIAEIDD AVKTNQVEIK EMEAKIAQLS AEKEASMGGE MKSLSEKVDA
LSQNLIVKNI EELKQSVDEK ASAVKKAEEG ASGLKNKVEE LTNSLEEHEK EYQGVLAGKS
SGNEEKCLED QLRDAKVAVG NAETELKQLK AKISHCEKEL KEKTNQLKSK REEANAVVKE
LNSRQKDVEN IRTGLESLSY KEGEMEDLQK ERTTEMDCVQ KWKDEIRNLS AYLANVEFTY
RDPVMNFDRS KVKGVVAKLI KVKDRSTMTA LEVTAGGKLY NVVVDTEKTG KQLLQNGNLR
RRVTIIPLNK IQSHPVPSRV QQAAVRLVGK GNAEVALSLV GYEEELKSAM EYVFGSTFVC
KTIDAAKEVA FNRDIYTTSV TLEGDIFQPR GLLTGGSRKG SGDLLGRLHA LAEAESKLSV
HQRRLSEIEA KISKLLPLQK KFIDLKAQLE LKSYDLTLFQ SRAEQNEHHK LGELVKKIEQ
ELNEAKSTIM DKQLLYEDCV KTVSSLENSI KDHDINRESR LKGLEKKIKS IKSQMQSSLK
DLKRHDSEKE RLVMEMEAVI QEQASLENQL ASLGALISNL TSDVEQQKFK VVAARDNLDQ
VQSELKSVSL KMKERDKEIS AIIKEQEKLE HKITESNLER KKMENEVKRM EMEQKDCSVR
VDKLIEKHAW IASEKQLFGR SGTDYDFSSC DPSKSREQLE KLQAEQSGLE KRVNKKVMAM
FEKAEDEYND LMSKKYIIEN DKSKIKKVIE ELDEKKKETL NVTWIKVNKD FGSIFSTLLP
GTMAKLEPPE GCSFLDGLEV RVAFGSVWKQ SLSELSGGQR SLLALSLILA LLLFKPAPLY
ILDEVDAALD LSHTQNIGRM IKAHFPHSQF IVVSLKEGMF NNANVLFRTK FVDGVSTVQR
TVASKQSK
//
