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Database: UniProt
Entry: A0A2H3D8C3_ARMGA
LinkDB: A0A2H3D8C3_ARMGA
Original site: A0A2H3D8C3_ARMGA 
ID   A0A2H3D8C3_ARMGA        Unreviewed;      1240 AA.
AC   A0A2H3D8C3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=ARMGADRAFT_995456 {ECO:0000313|EMBL:PBK90024.1};
OS   Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK90024.1, ECO:0000313|Proteomes:UP000217790};
RN   [1] {ECO:0000313|Proteomes:UP000217790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
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}.
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DR   EMBL; KZ293666; PBK90024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3D8C3; -.
DR   STRING; 47427.A0A2H3D8C3; -.
DR   InParanoid; A0A2H3D8C3; -.
DR   OMA; SYIRDHT; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000217790; 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; 1.20.5.340; -; 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; 2.
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:UP000217790}.
FT   DOMAIN          529..645
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          328..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          762..789
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          828..939
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1036..1077
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        333..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1240 AA;  139771 MW;  11EDB0FDA820F1FF CRC64;
     MPLVRIELCD FKSYRGHQTI GPFKNFTSII GPNGAGKSNL MDAISFVLGV KSAQLRSSQL
     KDLVYRGRKL AKGGAEEGTG SADEDDGDEG EGTARKAWVL AVYIDGAGKE WLFQRTISTT
     GASEYKLNGK VVTYTNYNAA LISHNILVKA KNFLVFQGDV EAVASQSPRE LAKLIEQISG
     SLELAAEYEK AKEGQERATE NATFNFSKRR GIAGEIKQYK EQKGEAERFE ALCQERDHLN
     LQRILFKLFH IEENIDSNSR EITTQNRALA GLRDEQRIHD QALDTARADQ AKSRTSVMQM
     EKKIKKADKT LEGKKPDLAA LEAQIAHSTR KMNKAKQTKE EVEKTERDVS ERVNKLQNEL
     GNVQKAANVA QEAQRLASQH NMALSEDSLE EYARLKASAS SLAVDERQSL EMLTRDEKTS
     GRTLNLLREK QQSYTEKRNQ RIEDSRVQTE KKTELEQKIS TLQAELAATK QELDNQQSER
     TKIAQLEAQA NEKLQHIYQQ LLQAGVDQHE SEKEAKLKET LANLQRLFPG VRGRVVDLCK
     PSQRKYDTAV SVVLGRNTDS VVVDEERTAI DCIEYMRTQR AGQATFIPLD TIQVKPVNDK
     FRSFAKGARL ALDVIQYEPA VERAMHHACG NALVCDTMEV ARMVCYEKGQ EVKAVTLEGT
     IIHKSGLITG GRSTHGGGKK WDEKDVQGLK RQRDSLLSQL RDLSKQKPRG KNDDNLFAEV
     SRLESAITIA KDDLTACKLR LTGIKDELRH IDKELKNNTP ELKKVESAYD KLQGQITNLK
     SSIDAAEDRV FSSFCRKIKV SHIREYEERQ LKVAQEESEA RLRYDSQIAR LTHQRDFESE
     ALESARERLQ HLEGVISTEE GVLEKLKDQK EAAENDISNS EAMIASLKEE LTTLQSALEE
     KTRHVDQVKK TTLKASKVLE QALKEITLRN DEIEKLALER SAIYRKCRLE EIKLPLLEGN
     LRNVPMEENL RDEVAMDVDE DEDGTQQPKR VDDFGIEVDF ESLDDDERED GSAEALAQFD
     ASISKLNGEI ERMAPNLKAM ERLDDVEAKL AETEKEADQA RKDSKNARDQ FQDIKKKRCD
     LFNKAYNHIS DRIDVVYKDL TKGKAAPMGG VAYLSLEDNE EPYNAGIKYH AMPPMKRFRD
     MEQLSGGEKT VAALALLFAI HSYQPAPFFV LDEVDAALDN TNVAKIANYI RAQASDSFQF
     IVISLKGSLY ERGNSLVGIY RDQEVNSSST LTLDLTQYDE
//
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