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Database: UniProt
Entry: A5E259_LODEL
LinkDB: A5E259_LODEL
Original site: A5E259_LODEL 
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
//
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