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Database: UniProt
Entry: A0A0S3T7M4_PHAAN
LinkDB: A0A0S3T7M4_PHAAN
Original site: A0A0S3T7M4_PHAAN 
ID   A0A0S3T7M4_PHAAN        Unreviewed;      1241 AA.
AC   A0A0S3T7M4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=Vigan.11G043500 {ECO:0000313|EMBL:BAU01243.1};
GN   ORFNames=VIGAN_11043500 {ECO:0000313|EMBL:BAU01243.1};
OS   Vigna angularis var. 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=157739 {ECO:0000313|EMBL:BAU01243.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAU01243.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   EMBL; AP015044; BAU01243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S3T7M4; -.
DR   Proteomes; UP000291084; Chromosome 11.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.1490; -; 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; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT   DOMAIN          553..669
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          214..371
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          446..536
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          719..840
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          877..988
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1241 AA;  141007 MW;  FB7A8324D2C10AAF CRC64;
     MNPHAESAPD SATRRRSARP RLFIKEMIMR NFKSYAGEQR VGPFHKSFSA VVGPNGSGKS
     NVIDAMLFVF GKRAKQMRLN KVSELIHNST NHQNLDSAGV SVHFQEILDL EDGTYEAVPG
     SDFVITRVAF RDNSSKYYIN DRTSNFTEVT KKLKGKGVDL DNNRFLILQG EVEQISLMKP
     KAQGSHDEGF LEYLEDIIGT NKYVEKIDES HNMLESLNEK RSGVVQMVKL AEKERDGLED
     VKNEAEAYML KELSLLKWQE KASKLALDDT SGKMDELQGN VVTVEENLKE ERDKIQESKQ
     TLKELETKHN NYMKRQEELE NDMRKCKEEF KEFERQDVKY REDFKHVGQK IKKLEDKVEK
     DSSKIEALIK EGEESTDLIP KLEDNIPRLQ KLLLDEEKIL DEITESSKVE TETYRSELAK
     VRSELEPWEK DLIEHKGKLE VACTESKLLN EKHERASQAF RDAQKQMENI SETIKSKTAS
     LSQIKRDIEK SKRDAAEAHR MEEECIKEQD ELIPLEQSAR QKVAELKSVL DSEKSQGSVL
     KAILKAKETK QIEGIYGRMG DLGAIDAKYD VAISTACAGL DYIVVETTNA AQACVELLRT
     ENLGVATFMI LEKQVDLLPT MKKKVSTPDG VPRLFDLVKV QDERMKLAFY AALGNTVVAK
     DLDQATRIAY GGNNEFRRVV TLDGALFEKS GTMSGGGGKP RGGKMGTSIR ATSVSVESVG
     NAEKELFELT AKLNDIRQKI VAAVQRYQAS EKAVAAFEME LAKSQKEVDS LSSQFNYIEK
     QLDSLEAASM PQEDELERLE ELKKIVSAEE KEIKRLTNGS KQLKEKALEL QRNLENVGGE
     KLKSQKSKVQ KIQSDIDKNS SEINRLKVLI ETGQKMVKKL TKGIEDSKKE EDRLTEQKQK
     LTGAFAEIEQ KAFAVQENYK KTQEIIDKHM TVLEEAQSKY NKMKKKMDEL RASEVDADFK
     LKDMKKAYKE LEMKGKGYKK RLDELQTAIH KHLEQIHADL VDQEKLEATL TDEHLNADCD
     LKKACEMVAL FEAQLKEMNP NLDSISEYRK KVSLYNGRVE ELNSVTQERD DIKKQYDELR
     KKRLDEFMEG FNAISLKLKE MYQMITLGGD AELELVDSLD PFSEGVVFSV RPPKKSWKNI
     ANLSGGEKTL SSLALVFALH HYKPTPLYVM DEIDAALDFK NVSIVGHYVK DRTKDAQFII
     ISLRNNMFEL ADRLVGIYKT DNCTKSITIN PGSFVVCEKA A
//
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