ID A5E259_LODEL Unreviewed; 1449 AA.
AC A5E259;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN ORFNames=LELG_03696 {ECO:0000313|EMBL:EDK45517.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK45517.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK45517.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; CH981528; EDK45517.1; -; Genomic_DNA.
DR RefSeq; XP_001524664.1; XM_001524614.1.
DR STRING; 379508.A5E259; -.
DR GeneID; 5232139; -.
DR KEGG; lel:LELG_03696; -.
DR VEuPathDB; FungiDB:LELG_03696; -.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; A5E259; -.
DR OMA; HEGNESG; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 755..871
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..735
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 918..1042
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1079..1162
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1256..1293
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1449 AA; 165768 MW; 49B7B6AE4A16C004 CRC64;
MKRKRPQIVD DEDSSSNDTF INNSDYDVKD LHEDVASDVD TSSIDQEQSQ EQMEMDERER
EEEEEEEEEE KKGDTKSLNL TTDSITKNLE NVDENALENE IDDKLQHSQN EESINKVDDD
PELTSRDSGH TQGLNSTNKL ITDVKQQRPA SAELTSSPTP RTTSTLASTS TSTSTPTATS
TNTATVENVT SIKENSQPLD DHKEITDEKS QHVPTHAHNQ PRLVIEKLVL TNFKSYAGCQ
TIGPFHSSFS SVVGPNGSGK SNVIDAMLFV FGFKATKMRQ GKISELIHNS GEEKPDFCQV
DIHFKQVIDD HEKSHKVDAP LDSELIISRK AYQNNQSFYY INDKKSTYTE VTSLLKNQGI
DLDHKRFLIL QGEVESIAQM KAKAEKEGED GLLEYLEDII GTTKYKQLIE NSTLEIEELN
TACQEKSARF DFVEKDKNLL DEKKAEALRF LEQEKKLSTL KGLKYQSKAR VYQGQIAAKE
EEVSELSKKL EEKRDSNREV LALIEADTKK QKEVKGEVKT LLAKIDKLNK EKKDLNKQNV
SFEEKTKSME TKLKKAQKAK NALTHSLNNA KQSLATYSNS SSQYTIEIDA LNVKFAEEEE
KLMRMRENLT ERTSGFTQEV ESLRKQMEPW TTALKENENN SQLLQSNIEL LESQMNAKKT
QLENSKQRLR QIKTEGKAKE AEYMEKESDL EKIEEQCALG EEQVNMLKSV LEKMKQQITK
QRNKLQDSLA IMQARDNKNS VLAALTKLGK SGRIEGFYGR LGDLGTIDEK YDVAISTAAP
GLDSMVVETV ETAQACIDYL RKNRLGYANF ICLDKLSKFD LSPIQVPGDP ARIKRLFDLI
KPSNSKFAPA FFSKMFNTLV APNLNEAKAV AYGARRWKVV TLDGKVIDTF GTMSGGGNYV
QRGAMKLSSA ERAQSREEDV DELDIEQMRS KLREMEEQLE ETNREYNESI AALKKVKALE
PETRLALDRL KLDIAGLASE MKDVSELRKS LIVEQEEMEI NNPFESQILE KKDQLEKLKR
EKLRLKEEMA ESEFRMSELE QKIMEAGGVE LKVQNSKVDS IKKQISIINE KTSGDRIAVK
KLESDILRHQ RLIEQAECEI KEFENALEDL KSSHKEIVSQ IHSLEEKIHA VEQEKIDKDE
QLEVLRVALE EKEEEISAFK QYEVETNNQL EKINGILRKI VYSMKECEKA FQSIEFRDAT
PYVYWLDEEE QARYIASDQD KLTDVEIDDI DLDAVESEIE EIEKYMSTIQ VDIEILKEYG
VKIREYNERR EDLNRAVEER DEKRDYCEDL KRKRLDEFMV GFSTISMTLK EMYRMITMGG
NAELELVDSL DPFSEGILFS VMPPKKSWRN ISNLSGGEKT LSSLALVFAL HKYKPTPLYV
MDEIDAALDF RNVSIVANYI KERTKNAQFI VISLRNNMFE LAQKLIGIFK YENKTKSVPI
LNIELEDIE
//