ID   A0A0D2CF17_9EURO        Unreviewed;      1183 AA.
AC   A0A0D2CF17;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 39.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=PV06_01033 {ECO:0000313|EMBL:KIW48452.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW48452.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW48452.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW48452.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) 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; KN847332; KIW48452.1; -; Genomic_DNA.
DR   RefSeq; XP_016268668.1; XM_016401615.1.
DR   AlphaFoldDB; A0A0D2CF17; -.
DR   STRING; 215243.A0A0D2CF17; -.
DR   GeneID; 27353107; -.
DR   VEuPathDB; FungiDB:PV06_01033; -.
DR   HOGENOM; CLU_001042_9_0_1; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000053342; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   CDD; cd03273; ABC_SMC2_euk; 1.
DR   Gene3D; 1.10.287.1490; -; 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; 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.
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   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT   DOMAIN          521..642
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          246..360
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          438..503
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          676..939
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1183 AA;  132568 MW;  F623DD487473C05F CRC64;
     MKIIELIIDG FKSYSQRTVI SGWDQSFNAV TGLNGSGKSN ILDSICFVLG ITNMSTVRAQ
     NLQDLIYKRG QAGVTKASVT IVFDNSDKST SPIGFEEYGQ ISVTRQIVMG GTSKYLINGH
     RAQQTTVQNL FQSVGLNINN PNFIIMQGRI TKVLNMKAAE ILAMIEEAAG TRMFEDRKEK
     AQKTMAKKEM KVVEIEGLLR EEIEPKLDKL RGEKRAWLDY QKTQSELERL TRVVVAADYV
     RAGDKMKSAN EEHETKRAKV QHLEENAIKL KREIENLDED AQRVRSVREK EMRKGGRFQE
     LENQVKELSH ELVRLSTVLD LKQSSVAEEE QRKKDIAKNV KNLEKQVADK KKSLEKLQSK
     WDGAKSELDA QHAEVEKKEE LLSTLQTGVA SREGQESGYQ GQLSEARNRL TTAGTEQEQA
     KLKISHLEKR IKEDEPRAKK AREQNAGLLK DLEVLRKQAQ KLEADLQKMG FDPGREEAMR
     EREVALQKSI RNLSQEADGL KRKVANVDFH FSDPSPNFDR SRVKGLVAQL FTLDKDKSMA
     GTALEICAGG RLYNVVVDTA ETGTQLLQNG KLKKRVTIIP LNKISAFKAS AAKVGAAQRI
     APGKVDLALS LIGFDDEVSA AMDYVFGTTL ICQDADTAKR VTFDPAVRLK SVTLEGDVYD
     PSGTLSGGSS PNSSGVLVIL QKLNEVTKEL EKHQAELREL QETMRNEQAK LASIKTVKEE
     LDLKTHEIKL AEEQISGNSS SSIIQAIEEM KASISQLKQD MSTARTRQEE AAKDVKRIER
     DMEDFSKNKD SKLKELEKSL VELKKSLTKT QGAIKALQRE LQDVRIDCEQ AESDLSAAEE
     QMVEVTNAIE VQKQELNTLR EEEASVKSNH DIAQAELTDE QAKLTGFDDE LRELEQAKSK
     KSKQISEEAL EAQKLGHAVE KAQKDAQAAS QLVTALEKEH DWIEDNKDQF GRAGTPYDFQ
     GKNLAESRAT LKNVTERFQG MKKKINPKVM PMIDSVEKKE TSLKNMLRTV IRDKKKIEET
     IVTLDEYKKE ALVKTWRKVT EDFGNIFSDL LPGNNTAKLV PLDDDINRIQ QGLEVKVCLG
     KVWKQSLTEL SGGQRSLVAL SLILALLQFK PAPMYILDEV DAALDLSHTQ NIGRIIKTRF
     TGSQFIVVSL KDGMFQNANR VFRTRFSEGT SVVTVMTPGE IKG
//