ID A0A0D1X5B4_9EURO Unreviewed; 1517 AA.
AC A0A0D1X5B4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=PV11_04957 {ECO:0000313|EMBL:KIV82891.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV82891.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV82891.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV82891.1,
RC ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
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; KN846952; KIV82891.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1X5B4; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000053599; 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:UP000053599}.
FT DOMAIN 762..875
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 483..552
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 581..615
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 641..745
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 915..1156
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 170467 MW; 47A0785A5D97F723 CRC64;
MSTITDSQSN CETSQRQIIE HTSGIMSAES PARPTRRAAR KTIVVEESED ELSQIQEDKD
EEFTPAPKRS PRKSTTRRQT TNSVSATPKR SARARKFKTG EGIEPTQIFD PEQSGGAPSE
PTSPTKTTSP RKRKSTSPRK GRRSSVVPPV PALPTPTASA SPEAEQTQTT PLRDITTKAL
NKNPPPQLQN DVLKETRPMD MGLEKPMDIV IRARSQAVPA VEEPIGSRSR MVIRQLVMTN
FKSYAGRQVV GPFHASFSAV VGPNGSGKSN VIDSLLFVFG FRASKMRQGK ISALIHNSAQ
HQDLDYCEVE VYFQEIIDLP GGKHEVVPDS QLVVSRKAFK NNSSNYYLNG RTTNFTTVTT
LLKDKGIDLD HKRFLILQGE VESIAQMKPK AANEHDDGLL EYLEDIIGTS RYKTPIEEAA
VELESLNEVC IEKQGRVQHV EKEKNSLEDK KNKALTFIRD ENELAEKQSA LYQIYTAECE
DNTKVTEEAI QQIQEQLDAE LEKHAGSEDT IKELEKAYNK AFKQYERIEK QAQEFTKELA
KYDKENVKFE EKRKFINGKQ KKAEKLATAS RLTMSEAQSL VEKHTCDIEK KSAEVVELEN
EMQKEEQELA VIRENLKGKT QGLSDQIAAK QKSLEPWNAK INQKQSEIAV AQSELDILKE
KASSGQKAID QANTKIESIE VNRSEKLEEI ERHKHDKARL EKDVRKIQDA LQKLAASEPE
VRSQISSARQ KADEARASLA SSQNQGNVLK GLLRLKESGR IDGFHGRLGN LGTIDEKFDV
AISTACPSLE NMVVDSVEVG QQCIDYLRKN NLGRANFILL DKLAQRDLSP IQTPENVPRL
FDLIKPKDAR FAPAFYSIMQ NTLVAQNLEQ ANRIAYGAKR WRVVTLDGQL IDVSGTMSGG
GTRVARGAMS SKLTSDTTKE QVQKLEGERD QLETQFEAFQ ARQRELESSL REKQEEIPRL
ETVIQKINLE VENCTRNLAD AQKRIQDLTA ELVSTAADDS QIKKLEKQIA LMNKELEKLH
SETASVEAEI QALQDKIMEV GGLQLRTQKA RVDGLKERID MLNDDISNAE VAKTKNEKLK
VKTEKAKDDA EQELESLFRD VEKLEADIEK HKAAAAESRS QAEQAQEEQA AMKEELAALK
KDLDAQTSEL NSTRAHEIEM KNKLEENQKV LADNNKKSRY WVEKLSKLTL HDVADLEGVP
EAQEEQPENR EIPLNEEEMP DAPPVADPDA MDVDEGDVPD MQDLKQEPQS EGRQGRRQLQ
TFTRDELADM SKDHLVASIA ALEEKVSTAS GIDLSVIAEY RRRCEEVASR TADLKNAVKT
RDTAKTRLTD LRNLRLTQFM TGFTTISSHL KSMYQLITLG GNAELELVDS LDPFSEGILF
SVMPPKKSWK NIGNLSGGEK TLSSLALVFA LHVYRPTPLY VMDEIDAALD FRNVSIVAGY
IKERTKNAQF IVISLRNNMF ELAERLVGIY KVNHMTKSVT VENRDYLAMA RQRELQEQRQ
RQGQDGQAVQ QSQGQIR
//
