ID A0A0N0NR94_9EURO Unreviewed; 1398 AA.
AC A0A0N0NR94;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=AB675_8631 {ECO:0000313|EMBL:KPI44569.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44569.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI44569.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44569.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-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}.
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:KPI44569.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFJN01000003; KPI44569.1; -; Genomic_DNA.
DR RefSeq; XP_018004532.1; XM_018149093.1.
DR STRING; 1664694.A0A0N0NR94; -.
DR GeneID; 28740973; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000038010; 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; 2.
DR PIRSF; PIRSF005719; SMC; 2.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000038010}.
FT DOMAIN 649..762
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 468..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 802..1043
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 606..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 155346 MW; BD7A26EA65DB66DF CRC64;
MASASPARPT RRAARRNVVV EEDSEDELSM VQEEPDQEFA PVPKRASPRK STRRQTSAEA
APSPKKSTRT RRTRASEGIE PSQIFDAEET VPSIEPPSPT KKVASPRKWK SAAPTRSRRS
SAVPSVTPAP QDDASEIGIQ LEAPSTPLAD ITSKALNRPP PSATKVKPVQ HVEPERVLEK
PMDIVIRARS QVLPVVEEPT GPKSRMVIRQ LVMTNFKSYA GRQTVGPFHA SFSAVVGPNG
SGKSNVIDSL LFVFGFRASK MRQGKISALI HSSANHPDLD FCEVEVHFQE IVDLPGGKHE
TPIEEAGVEL ENMNEVCIEK QGRVQHVEKE RNALEDKKNK ALTFIRDENE LVEKQSTLYQ
IYIAECEDNA QVTEEAVEQM QAQLNAELEK HAGEEDGIHE LEKAFKKGSK EFEAMTKATQ
ELAKDNAKHD KESVKFDEKR KFIAGKQKKA EKTLSSSRFA ASDAANSVEK HTDDIERKSK
EVAELEASMH KEEQELAVIR EGLKGKTQGF SDQIAAKQKS LEPWNEKVNQ KQSQAAVLQS
ELDILLEKGK SGQKAIEEAQ AKIESIQTQQ SEKAAEIEQR QKEKARLEKD IRKHQDALQK
LAASEPEVRS QVSSARQKAE EGRASLQTSQ NQGNVLKGLL RLRDTGRIDG FHGRLGNLGT
IDQQYDVAIS TACPALENMV VDTVEAGQQC IEHLRKNNLG RANFILLDRL AQKDLSPIKT
PENVPRLFDL IKAKDKKFGP AFYSIMRDTL VAENLEQANR IAYGAKRWRV VTLDGQLIDV
SGTMSGGGTR VARGAMSSKL SSDTTKEQVQ QYEAERDAIE QQFDAFLERQ RDLENSLREK
QEELPKVDTA IQKCNLDVSN LSRNLVDAEK RVQDLTAELN NTSADDAQIK SLEKQIANTR
KEIDSLKAET AMVEGEIEAL QNKIMEVGGL RLRSQKATVD GLKERIDLLN EDISTAEVGK
TKNTKLHTKH EKARADAEKE LETLATDLEK LEADVAAQAT NTSDSKQRLQ AAQDELSVKK
DELAEIKSSL DKQTAQLNET RAAEIEMRNK LEENQKILGD NSKKNRYWKE KLSKLELHDI
ADLEVPVEAP AVPDENAMDV DQAEEGTTKA VEALGADADA MDVDGAPPTS PSQHDTSIQQ
SRRQLPIYTR DELEDKSKDH LVASIAALEE KVSNASGIDL DSAKNRLTDL RSMRLTQFMT
GFTTISQHLK SMYQLITLGG NAELELVDSL DPFSEGILFS VMPPKKSWKN IGNLSGGEKT
LSSLALVFAL HVYRPTPLYV MDEIDAALDF RNVSIVAGYI KERTKNAQFI VISLRNNMFE
LAERLVGIYK VNHMTKSVTV ENRDYLGMQR EERLRAARAA QARALALQQQ TQTQRPGTAG
SLGSSQVPQQ KTQQQSSQ
//
