ID   V9DLA5_9EURO            Unreviewed;      1183 AA.
AC   V9DLA5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   13-SEP-2023, entry version 42.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=G647_09616 {ECO:0000313|EMBL:ETI27426.1};
OS   Cladophialophora carrionii CBS 160.54.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI27426.1, ECO:0000313|Proteomes:UP000030678};
RN   [1] {ECO:0000313|EMBL:ETI27426.1, ECO:0000313|Proteomes:UP000030678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI27426.1,
RC   ECO:0000313|Proteomes:UP000030678};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL   Submitted (MAR-2013) 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; KB822698; ETI27426.1; -; Genomic_DNA.
DR   RefSeq; XP_008723832.1; XM_008725610.1.
DR   AlphaFoldDB; V9DLA5; -.
DR   GeneID; 19988109; -.
DR   VEuPathDB; FungiDB:G647_09616; -.
DR   HOGENOM; CLU_001042_9_0_1; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000030678; 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}.
FT   DOMAIN          521..642
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          343..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..290
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          403..503
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          680..939
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        353..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1183 AA;  132456 MW;  B1714BA7146F6DE9 CRC64;
     MKIIELVIDG FKSYSQRTVI SGWDKTFNAV TGLNGSGKSN ILDSICFVLG ITNMSTVRAQ
     NLQDLIYKRG QAGVTKASVT IVFDNSDKST SPIGFEEYAQ ISVTRQIVMG GTSKYLINGH
     RAQQTTVQNL FQSVGLNINN PNFIIMQGRI TKVLNMKAAE ILAMIEEAAG TRMFEDRKEK
     AVKTMAKKEM KVVEIEGLLR EEIEPKLDKL RGEKRAWLDY QKTQSELERL TRVVVAADYV
     RAGEKMKNAS QEHEAKRAKV THLEENAIKL KREIENLDED SQRVRAVREK EMRKGGRFQA
     IEAQVKELSH ELVRLATVLD LKQSSVAEEE QKKKDVTKNV KSLEKQVSDK KAGLEKLQSQ
     WNSAKAEHDS QNSEVEKKEE LLSTLQTGVA SREGQESGYQ GQLQEARARL TAATTEQEQA
     KLKISHLEKR IKEDEPRAKK AREQNADLLK DLEVLRKDAQ KLENNLQRLG FEPGREEKMR
     EHEVTLQKSI RELSRQADEM KRKVANVDFH FSDPSPNFDR TRVKGLVAQL FTLDKDKSMA
     GTALEICAGG RLYNVVVDTA ETGTQLLQNG KLKKRVTIIP LNKISAFRAS AEKVGAAQRI
     APGKVDLALS LIGYEDEVSA AMDYVFGTTL ICQDAETAKK VTFDPSVRLK SVTLEGDVYD
     PSGTLSGGSS PNSSGVLVIL QKLNEVTKEL QKHQSELQQV QETMRQERAK LADIKSVKQE
     LDLKTHEIKL AEEQISGNSS SSIIQAIEEM KATIVQLKQD MANAKTREVE ASKDVKRIEK
     DMEDFSKNKD SKLKELEKSI AELKKSLTKT STAIKSLQKE LQDAKIDCEQ AESDLNAAVE
     QLAEVNATIE TQKAELEALR QEEASVKSNH DMAQGELVDE QAKLTGFDDE LRELEQAKSK
     KSKQIAEEAL EAQKLGHAVD KAQKDAQAAA QLVAALEKEH DWIDDNKDQF GRAGTPYDFH
     GKNLAESRAT LKNVTERFQG MKKKINPKVM PMIDSVEKKE ASLKNMLRTV IRDKKKIEET
     ISTLDEYKKE ALIKTWRKVT EDFGNIFSDL LPGNNTAKLV PLDDNLERIQ EGLEVKVCLG
     KVWKQSLAEL SGGQRSLIAL SLILALLQFK PAPMYILDEV DAALDLSHTQ NIGRIIKTRF
     QGSQFIVVSL KDGMFQNANR VFRTRFSEGT SVVSVMTPGE LKG
//