ID A0A0D2ART0_9EURO Unreviewed; 1476 AA.
AC A0A0D2ART0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=PV07_07525 {ECO:0000313|EMBL:KIW27822.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW27822.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW27822.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW27822.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; KN847043; KIW27822.1; -; Genomic_DNA.
DR RefSeq; XP_016248038.1; XM_016394619.1.
DR STRING; 569365.A0A0D2ART0; -.
DR GeneID; 27346719; -.
DR VEuPathDB; FungiDB:PV07_07525; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000054466; 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; -; 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; 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.
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:UP000054466}.
FT DOMAIN 735..848
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 23..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..423
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 449..525
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 561..588
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 614..718
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 888..1122
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 165875 MW; 8924F79D011EFEB3 CRC64;
MSAESPARPT RRAARKNVIV VDSDDELSLI KEDDDEEFTP APKRSPRRST RRQTTANVDA
SPKKSARSRK FKTGEGIEPS QIFDPEETMP SSSPTSPTKT ASPRKRKSVA PRKSRRSSVA
PPLPELLPPD STTSSAHDTL PGTPLKDITS QALNMNAPLE ADHELRKPIR PADPMLEKPM
DIVIRARAQA VPIAEEPTGP KSRMVIRQLV MTNFKSYAGR QVVGPFHASF SAVVGPNGSG
KSNVIDSLLF VFGFRASKMR QGKISALIHN SAHHQDLDFC EVEVYFQEIV DLPGGKHEVV
PDSELVVSRK AFKNNSSNYY LNGRTTNFTT VTTLLKDKGI DLDHKRFLIL QGEVESIAQM
KPKAANEHDD GLLEYLEDII GTSKYKTPIE EAAVELESLN EICVEKQGRV QHVEKEKNSL
EDKKNKALAF IRDENELAEK QSALYQIYIA ECEDNTKVTE EAIQQIQEQF NAELEKHAGN
EDAIRDLENA YHKAVKQYER IEKQVQDLNK ELAKFDKESV KFDEKRKFIS GKQKKAEKTA
TSSRLAASEA QSLVERHAGD VQRKGAEVLE LEKEMEQEEK RLAVIRDDLK GKTQGLSDQI
AAKQKSLEPW NAKINQKQSA IAVAQSELDI LKDKANSGQK SIDQANERIA SIETDKTTKL
EEIEQRKYEK ARLEKDIRKI QDALQKLAAS EPEVRSQISS ARQKADEARA SLATSQNQSN
VLKGLLRLRD SGRIDGFHGR LGNLGTIDEK FDVAISTACP SLENMVVDNV EVGQLCIEYL
RKNNLGRANF ILLDKLAQRD LSPIQTPENV PRLFDLIKPK NERFAPAFYS IMQNTLVAQD
LEQANRIAYG AKRWRVVTLD GQLIDVSGTM SGGGTRVARG AMSSKLASDT TKDQVQKLEN
ERDQLEKQFE AFQTRQRELE ASLREKQEEI PRLETAIQKT NLEVETCTRN IADVQRRIQD
LTTELASTSV DDSQIVRLQT HIESMNRELE QLHSETASVE AEIQALQDRI MEVGGIQLRT
QKARVDGLKE RIDMLNDDIS NAEVAKTKKE KLKVKNEKTK SDAEKELESL SRDLEQLEQD
IERHKSAAAE LRAQVDKAEE QQSNMKDELG DLKKNLDAQT AELNSTRAVE IEMKNKLEEN
NKVLADNQKK SRYWTEKLSK LTLHDTADLE ALSQDQDRQQ PQRPADEDMP DAPPETDPDA
MDVDEGQHEE QPKTPSTPAR RQLQTFTRDE LLDKNKDHLV ASIAALEEKV SNASSIDLSV
IAEYRRRCEE VASRTGDLKN AVKSRDAAKT RLTDLRNLRL TQFMTGFTTI SSHLKSMYQL
ITLGGNAELE LVDSLDPFSE GILFSVMPPK KSWKNIGNLS GGEKTLSSLA LVFALHVYRP
TPLYVMDEID AALDFRNVSI VAGYIKERTK NAQFIVISLR NNMFELAERL VGIYKVNHMT
KSVTVENRDY LAMGGRRQEQ PTSDGRTTTG QPGQIR
//
