ID R9AP05_WALI9 Unreviewed; 1276 AA.
AC R9AP05;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=J056_004057 {ECO:0000313|EMBL:EOR01821.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR01821.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007229; EOR01821.1; -; Genomic_DNA.
DR RefSeq; XP_009267541.1; XM_009269266.1.
DR AlphaFoldDB; R9AP05; -.
DR STRING; 1299270.R9AP05; -.
DR GeneID; 20377009; -.
DR KEGG; wic:J056_004057; -.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR OMA; CPALDNM; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000014064; Unassembled WGS sequence.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR Gene3D; 1.10.287.1490; -; 2.
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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064}.
FT DOMAIN 560..673
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 309..399
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 723..750
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 803..837
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 881..950
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1056..1124
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 492..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 143419 MW; 4C2B1D79B2E87546 CRC64;
MSDDVLGESN KQPEQPEQPE EKPKRSRLVI HQLALINFKS FAGTQVIGPF HKSFSSIVGP
NGSGKSNTID ALLFVFGYRA NKMRQSKLSE LIHNSAEHPN FDHCAVEVHF REIFDEPGSE
DFQIVPNSQL VVTRMAMRNN QSKYLIDGES SNYATVTNLL KGRGIDLDHN RFLILQGEVE
SIAQMKSKAP SPHEDGLLEY LEDIVGTVTY KQPIEDSLVD MDKLSDERSE RLSRLRIVEK
EKDRLEGHKD EAESYLKDCN SVARKKNVLY QRYLFDLTNN ISVCNEHLQE ISTQLHSEES
KVSGRKDALC DLEAEHKRLE KECKGMESEM KRITKSHEDK NKENVKLDVK MKDLNSKIKK
LKKSLADDSH AHKTAQHNIT ELTEEMEKAR AETESHEAGL GAEEGKLESI IDSLKGKTQV
FTDQIESKQK ELQPWQAKLS DLQTKIDVAD SERDLLSSKA DSAQKAAAEA DEQLQAVKDQ
VETKKSSATD IQSERQRVSA EMSQLESQLS DLRKEEGNMR RHLSQARHKA DEARSSLTAN
RSQDAVLASL TRLRDTGRVS GFHGRLGSLG VIHDKYDIAI TTACGGLNNF VVDTVQAAQT
CIAHLRENNV GRATFIVLEQ LAGKTPVKLA TPEDAPRLID LVQPRKKEYI PAFYKALGNT
LVAQDLTQGN RIAYGKNRWR VVSLQGNVIE ASGAMSGGGQ RVLRGGMGSS FANPTDTVTM
DTVNQLESER EKVEEKLREI LEKVASIENE CGGLRKLAPE LEIQAEKAEL DQATFTKRIS
EAEKHARKMK EESKPDAGDS KRIKSLDTEM SKLKKEVDKL VDKTSSIESE IEQLQEKILE
VGGVKLRAQK SKVDSTKMMM GLCSERITKA EVSLSKSNKD ISRYAKSVKD NEKKLAKLEE
EISAVSEKND QQLSKAKGVR SEVDKVRDAL EGKQEELNEV KAQLDNEALA MQSFNALETD
LKGQMDETTN ILKDSENKIG IYRERLGKLT LQDVDDEEEQ ESALAQSDEP SIQQEGEGEG
DEKMEEDEAS LPQPQPTQTK QPPKPASAQL ETYSQEEIQE IQLDVLKKEI VRAEDKVEKS
TVNLEVLAEY KSRKKEYRDR AADVQDVTRR RDEAKSTYDE LRKKRLDEFM HGFTIISSKL
KEMYQMITLG GNAELELVDS LDPFSEGIIF SVMPPKKSWK NISNLSGGEK TLSSLALVFA
LHAYKPTPLY FMDEIDAALD FRNVSIVANY IKDRTKDAQF IIISLRNDMF ELSNRLVGIY
KTMNATKSLT IANTNL
//
