ID F0WE71_9STRA Unreviewed; 1192 AA.
AC F0WE71;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 22-FEB-2023, entry version 48.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=AlNc14C72G4927 {ECO:0000313|EMBL:CCA19500.1};
GN ORFNames=ALNC14_056430 {ECO:0000313|EMBL:CCA19500.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA19500.1};
RN [1] {ECO:0000313|EMBL:CCA19500.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA19500.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; FR824117; CCA19500.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WE71; -.
DR EnsemblProtists; CCA19500; CCA19500; ALNC14_056430.
DR HOGENOM; CLU_001042_9_0_1; -.
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:0030261; P:chromosome condensation; 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; 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; 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; 2.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
FT DOMAIN 523..645
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 316..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..450
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 694..866
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 990..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 323..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 136461 MW; A2CB0C8E0421A347 CRC64;
MHIEEIIIDG FKSYATRTVI SGFDPHFNAI TGFNGSGKSN ILDAICFVLG ISNLSQVRAG
NLQELVYKQG QAGITKATVT IVFDNHNSNA SPVGYEQYEQ ISVARQVIIG GRNKYMINGH
TAQVSQIQNL FHSVQLNVNS PHFLIMQGRI TKILNMKPLE ILSMIEEAAG TRMYETKKQA
ALRTMIKKDR KVEEINAILA EEITPTLEKL RQEKQQYLVW AANNTELERL ERFCIAYKYQ
KAVDVINTVD ANVQQLEQNF ESSRQREKKL QDRIEALDVE IDRIEREKQQ KGGPNLQILK
EKVNQLDQQV AKIHTQHQNV ESQIKAQEEK QRITSEQRKD AEQSMKKLRR EMEMKQKEVA
SSKTKLEAIK EKKKSVHDEM QALNAGITQT KGPTKASFVE DLAERQKELQ EENTIQQQTA
LKIKHLEKQC KQQRTRLDQS KHDNRNLVQE QTQNRAEVDA LNAKMDSITS TFDPTEEKAV
HHAMKQLRID IRQNECQIDE LSSSLSSRLD FHYSDPYPNF LRESIKGVLA KLLETKHEWS
ALALEIVAGG KLYQVVVDNE KIAKDILKHG RLMNRVTIIP LNRISRRIIE PFKIQKAQKI
AEKSGGKIWE ALELIHFDQA VQPAMEYAFG NSIVCETSEI AKEVTFHRDI KVRTVTLDGD
SFDPAGTLQG GSAPSNGPPM LLKLHSLLQS TRTLQSLRDE LSSKQARLEQ LRQDGEQYRA
VQSQLELKKH QLVLIDERIS QSAHAQQERD VSLAESELQE ANDKLTETSS RIESLLDSIK
TIKQKIQSVK QSRSTRIQAL EDELKALTIQ TQQAQNHYKS IKQQHSESEL EIESLVQEIQ
TSDAAMQKID KKIARLRHDA QQLVDQQSTT EGDLREATLQ WDQHREMIQE SDQKLRLLVE
KRAKFSRKKT ECEVSKKKHE HRKQRLFREK EDSTALVREM EQEHAWISAE KEFFGREHTD
YDFEKQDSES VMQRRILLKK EQDAISLKIN KKVVGMIEKA EQEYQSLMTK REIIEKDKEK
ITFVIEELDT KKDEALKTTW RKVNKDFGSI FSTLLPGTTA KLEPVDSETV LDGLQVSVAF
GGVWKESLTE LSGGQRSLLA LSLILALLLF KPAPMYILDE VDAALDLSHT QNIGQMIQSH
FSQSQFIIVS LKEGMFNNAN VVYRTKFVDG VSTVTRTVPS KKQKRQSESP AN
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