ID A0A1S3UZF6_VIGRR Unreviewed; 1804 AA.
AC A0A1S3UZF6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Sister chromatid cohesion protein {ECO:0000256|RuleBase:RU364107};
GN Name=LOC106770121 {ECO:0000313|RefSeq:XP_014511435.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014511435.1};
RN [1] {ECO:0000313|RefSeq:XP_014511435.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014511435.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364107}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family.
CC {ECO:0000256|ARBA:ARBA00009252, ECO:0000256|RuleBase:RU364107}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014511435.1; XM_014655949.2.
DR STRING; 3916.A0A1S3UZF6; -.
DR GeneID; 106770121; -.
DR KEGG; vra:106770121; -.
DR OrthoDB; 1409889at2759; -.
DR Proteomes; UP000087766; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21704:SF18; NIPPED-B-LIKE PROTEIN; 1.
DR PANTHER; PTHR21704; NIPPED-B-LIKE PROTEIN DELANGIN SCC2-RELATED; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU364107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364107};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364107};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 659..708
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 126..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1804 AA; 201034 MW; 6AF8D066707DB39B CRC64;
MSFPVTSGAG VAAAFSGSRG IGLSNTVHSE LAACLPLPSL PVFCGASDQD LRLVDSPARL
NRVDVLAQSG KIAELLRHTD VSYLNLRDEA KGVPYIYVEP LELHDEVLRC NPEAFEYSTA
GPVKEQISGS AVPEKRQSES SFSVPSQTQK DYNATHSRQL DNFSTNDISA LSSKKSKVKK
KGGDGISIAP DSAELQGAHI QRFCDLLEDL CSKSELNSDD RDEAEWLSLP LSDLRLLVNE
ITSIREKKLL HLVPIEVLVR LLKVLDHQIH RAEGLSIEEC DNSSDSELVS SVFIALESIH
AALAVMAHSD MPKQLYKEEI IERILEFSRR QIMDVMCACD PSYRALHRPG ENTGFEVDDY
EENDAEFGSA SKKRRTNKTL KLKKSATSRV STAVNTILQK LCTVLGLLKD LLLIERLSDS
CILQLVKTSI TTFLVDNIQL LQLKAISLLS AIFYLYVQHR IYVIDEMVQL LWKLPYSKRA
LRSYHVREEE PRQIQMVTAL LIQLIHCSAN LPDALRKASN GNSVLEASVD ASTPIKSHEA
VTEACCLFWS RVLQRFASVK TQDASELKSI IENLVTDLLT TLNLPEYPAS ATILEVLCVL
LLQNAGPKSK DVSARTMAID ILGTIAARLK RDALVCSQEK LWILQDFLSP DAHAEHQSKD
ICCVCLGGRV ENLFTCHGCQ RLFHADCLGI KEHEISSRNW SCQTCICHKQ LLVLQSCCNS
QHKNNVKKNS KASKDSEVST QDIVQQLLLN YLQDVTSPDD LHLFICWFYL CLWYKDDSNF
QQKSIYYIAR MKSKIIVRDS GAVSSMLTRD SIKKITLALG QNSSFCRGFD KILHTLLASL
RENSPVIRAK ALKAVSIIVE ADPEVLGDNR VQSAVEGRFC DSAISVREAA LELVGRHIAS
HPDVGFKYFE KIAERIKDTG VSVRKRAIKI IRDMCTSDAN FSGFTRACTE IITRVSDDEA
SIQDLVCKTF SEFWFEEPHA PQTHSFGDGS TVPLEIVKKT EQIVQMLRGM PNNQLLVTVI
KRNLALDFLP QSAKATGISP VSLATVRKRC ELMCKCLLEK MLQVEEMNSD EVEVRALPYV
LLLHAFCLVD PTLCAPASNP SQFVVTLQPY LKTQVDNRMV AQLLESILFI IDSVLPMLGK
LPPIIVGELE QDLKQMIVRH SFLTVVHACI KCLCSASKMS GKGAVVVEQL VQFFFRCLDT
QAVDNKQKVG RSLFCLGLLI RYGNRLLANS GNKLVDFGSS VRLFIKHLSA EDFVVKVRSL
QALGFVLIAR PEYMLESYVG KILEETLSSA ADTRLKIQGL QNMYEYLLDA ESQMGTDKDD
DNVAGYTVGA GQSVPVAAGA GDTNICGGIV QLYWDNILGR CLDFNEQVRQ SALKIVEIVL
RQGLVHPITC VPYLIALETD PLESNSKLAH HLLMNMNEKY PAFFESRLGD GLQMSFMFMQ
SICGGSENVD TKIQSKMPIS GKGKPEAGLL AQAKLGVSRI YKLIRGNRVS RNKFLSSIVR
KFDNPRWNKL VIAFLTYCTE VLALLPFISP DEPLYLIYAI NRIVQVRAGL LEANFKAWTS
SISNHGTPYG NGMHQQAPEE STVTIQAMSV DLNGSIQQNI YAHLNSNDLR SLDLNGSNHQ
QVDYSHTGSP ETKPHAAGYT DFNFSKDDLE KVQADCLSAI ALQLLLKLKR HLKIMYSLDD
ARCQAYSPTE QPKPGEVISR QNIAFSLGES QFSLPTTPQE LVPRYQEFKH ALREDTVDYS
HYTANIKRKR PTTTPRKVQA RKAVHVSSGN YNEEDDEDYG GGSSMRNITF GGSRRSSLRS
SRQY
//
