ID A0A0M8MMS6_9BASI Unreviewed; 1222 AA.
AC A0A0M8MMS6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=Malapachy_2713 {ECO:0000313|EMBL:KOS15636.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15636.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15636.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15636.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS15636.1}.
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DR EMBL; LGAV01000002; KOS15636.1; -; Genomic_DNA.
DR RefSeq; XP_017993268.1; XM_018137201.1.
DR AlphaFoldDB; A0A0M8MMS6; -.
DR STRING; 77020.A0A0M8MMS6; -.
DR GeneID; 28729076; -.
DR VEuPathDB; FungiDB:Malapachy_2713; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; 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:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF12; 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|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 519..635
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 307..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 393..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..929
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1019..1060
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1222 AA; 138707 MW; 5A7DF07B8A0B7433 CRC64;
MPLKQLEIDN FKSYRGKQIV GPFSAFSAVI GPNGSGKSNL MDAISFVLGV RGAQIRSSEL
SDLIYSRNLS QGDTVTVFED DAPSKASVTA VIEDANHMEH RFQRIVTATG ASEYRYNGRM
TTQASYNAKL EQLNILVKAR NFLVFQGDVE AFAEQCSKDL SEVIDQISGS KLLQGEYEAA
KSAYQEAVDH SAALVAKRKT LQGELRHMRQ HKEASDRYDV LKNELSSHIV QKMLWRLYHI
HEIIEIHTDW IEAHATRGEQ ARKRLEDKEG IVAAARTELG KVQQAVLDKE NEKKQTARLL
DAKRPEKDRL VERAEHARRK LQQAQSLYKQ AEKDHTVQAE ALNRLEADKV LVEKALVQAK
EAQEAALATT TRKLSDEELQ MYHALKAQSA AIASDERTQL EQIQRERREK QTALDTVQDR
LDDAASKLER LEEQEALLAA SAMSLEQREP EAAEKVKEAK AALEQHQAQK EDIAAREKEL
NDVLVLCYNK LLRMGQDQRV HEREMRLRES IRSLRSIFPG VHGRLLDLCK PTQKKYEIAM
ATTLGRNTEA VVVDHESTAM ECIEYLRNQR AGQATFIPLD TIQTKPINDR LRSVSPQARL
AVDVMQYSPA VERAVHFACG NTLICDTLDV ARNVCFEKNQ RVKAVTLDGT VIHKTGMMTG
GPSMQDSVRQ WDEQEMLGVQ RERDRCMSEL KELQQQKYTL GEEEEAVAKI TRAQAALSNV
HQEQADVARR RKDIAAERST LEAQQKALTV DVHKHNTALT TLATRLTELE TFLAQVDDKH
FAAFCERIGV ANVREYESQQ LALTQALDME TEQYQRQLAR LAHQRTFTLQ QEQNTAERLA
YIQAAIDKET KRLPALEQEM AACDREMASL RAQLEQMQSD WQALRDQHRE KSDALHEKRK
ALIATSRDVD AHRKEVAERN DEIAQLDLER TNLYRQCRLE TIDLPLESGD LANVALEDEA
PLPAVDGDDA VQPIRPFDVV VDFSRLSDAE RTDRGSTKAR ELQDKIDMAR EEMAKLNPST
HTANKLEGLE RELQTCERDM DSCREHVRET REELQHVKKQ RTDKFMRAYN HIAERIDGVY
KDLTKSKAAP MGGVAYLTLE DTDEPFRTGI RYHAMPPMKR FRDMDQLSGG EKTMAALSLL
FAIHTYQPAP FFVLDEVDAA LDSQNVARVS EYIREHASDQ FQFIVISLKA SLYERSQGLV
GVYRNQAANS SAIVTLDLES YA
//
