ID A0A177C3U4_9PLEO Unreviewed; 1180 AA.
AC A0A177C3U4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=CC84DRAFT_1127333 {ECO:0000313|EMBL:OAG01552.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG01552.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG01552.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG01552.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441557; OAG01552.1; -; Genomic_DNA.
DR RefSeq; XP_018031917.1; XM_018175768.1.
DR AlphaFoldDB; A0A177C3U4; -.
DR STRING; 1460663.A0A177C3U4; -.
DR GeneID; 28759254; -.
DR InParanoid; A0A177C3U4; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000077069; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 521..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 387..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 239..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 326..374
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 415..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 682..945
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 387..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 132686 MW; CE60A26A34A3432B CRC64;
MKIVELVIDG YKSYATRTVI RDWDSSFNAI TGLNGSGKSN ILDSICFVLG LTNLSSVRAS
NLQDLIYKRG QAGVTKASVT ITFDNRDKAN SPETHKNVDT ISVTRTIVIG GTTKYLINGM
RAQQHLVHSL FQSVQLNINN PNFLIQQGYI TKVLSMKPKE ILSLLEEAAG TRMYDDRRDK
ALKTLTKKEL KVQELNGLLT DEIGPKLDKL RQEKRAFLDF QQTQGDLERL IRLVVAYDYV
NYKEKLRQSL DDLEAKKQRA DFLEQSAARM KGEIEYIQED IEKVKATREK ELRKGGQFQA
LDEEVKTHSH ELVRLTTVLD LKKSSISEEV DRKRNIEESV QDLEKQLQEK IKAHEKLEQK
YNAAHDELAK QTADVSEKEE LLQTLQTGVA SKEGQESGYQ GKLQEARNRE SAAAIEQEQS
KLKIAHLEKQ IKEDEPKAKK AKEQNSGLLK ELEAQKLQAK RLEAELSKLG FDAGHEAELY
QQESHLQTRI QDLRREADAL KRKVANIDFS YENPSPNFDR SRVKGLVAQL FTLDKDHTRA
GTALEICAGG RLYNVVVDTA ETSKQLIQNG RLKKRYTVIP LNKIKAFKAS AEKIGAAQRE
APGKANLALS LIGYDDEVSV AMEYVFGNTF ICEDAKTAKA VAFGGPRTKS VTLEGDVYEP
QGTLSGGSAP QTSGVLVTLQ KFNEITGELQ AQEQQLAELQ ATMARERKKL DGAKRLKQEL
DLKTHAIQLT ESQISGNSSS SIIQAVEEMK KSIGQLKDDI KAAKSRQDEA SKDIKRVEKD
MKEFNSNKGS KLAELQSSLD KLKKALAKNS ASLKPLQAEN REAKVVVDHI AGDLAAAKEQ
LEEAQTTLSS SQEEIDALVA EQARVKHDHD VAQANLADEQ KKLTSFDDEL RALEDAIKTK
NSSITEAKLE QQKLGHEIER FDKERDEASG RIEALEKEHD WIELESEQFG RSGTIYDYRG
QNMSDCKSRR KTMDERLRGM KNKINPKVMA MIDSVEKKEV SLKKNMSIVI KDKQKIEETI
KKLDRYKHEK LEETWAKVNG YFGTIFNDLL PGAFAKLDPL EGKSVSEGLD IKVMLGKVWK
QSLTELSGGQ RSLAALALIL ALLQYKPAPM YILDEVDSAL DPSHTQNIGR IIKERFTESQ
FIIVSLKDGM FDNANRLFRI YFADGTSKYE IMPTKGAARR
//
