ID A0A0C9XR68_9AGAR Unreviewed; 1596 AA.
AC A0A0C9XR68;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN ORFNames=K443DRAFT_679375 {ECO:0000313|EMBL:KIK00197.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK00197.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK00197.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK00197.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; KN838631; KIK00197.1; -; Genomic_DNA.
DR STRING; 1095629.A0A0C9XR68; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000054477; 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:0051276; P:chromosome organization; IEA:InterPro.
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; 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 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT DOMAIN 858..973
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 512..641
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1173..1284
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1596 AA; 178558 MW; B6ECEB484725AAA6 CRC64;
MPPRRSSRAP SSHVEPPVAE ILPGKRKRGQ TANPEPEEKE NVAKPASRTT RRSSSARPSV
APPPKGRVAS RSKVLPDVQE SGDEEHEEEP PIKKSRPSVD AEAQEEEDEE EVQPAKGRKS
TKGRGVKMEV EVLANPKSRR SSSRQAVNVS SGSRSSAAGS SRSKIAPVEE SAAEDDEEEE
EKPKPARRGR ASAKPAARKS SKAKPISDNE ESDAATPASD DEDDEEKIKP ARKGRKPKAA
AAARKSRAPA KKAPKPAVAD DSDEDIEAPP SAQLRQAPMD VEAPTPSAPP QEEEEEKSLF
DPPPMPAPSS LPTTMPEEPS GPKSRLVIHK MALVNFKSYA GRQEIGPFHK SFSSIVGPNG
SGKSNTIDAL LFVFGYRASK MRQAKVSELI HNSARYPDLD ECSVEVHFRE ILDLPGPDAF
KVIPGSKLVV SRQAYKNNQS KYTINGRTST YSEVQTLLKG RGIDLDHKRF LILQGEVESI
AQMKPKAPTE HEDGLLEYLE DIIGTSKYKE PIDEALVKME QLQEERQVKL NRLRLVEKEK
SALEAKKREA EDYLRLKNEH VRALSRLWQW YLWQGLMHEE QAQLDVEKYQ KMLAEETDKN
KDDITHLEML RKHFRQREAA YEEVNKAAAA AVKELAANER QEVSLTERRK HAAGREKKLK
KSLQEDKTAM TTALRAVEES ADKIKRNKVK VEEHEASLLE EEKILEGIRD SLKDKTQVFH
DQIEVKQKEL QPWTAQINSK RAEVDVATSE RDALAKKAAV LKASSEEAEE NLRTLQTDQQ
KNLDIQNRHK TEKANLQRQT QEARKRFEDA QKQVNELRNK ANAARNKVEE AKASQSQNRS
QGAVLDTLSQ LQRSGRIQGF HGRLGALGTI PDKYDVAIST ACGGALSNMV VDTVNQGQDC
IAYLRKNNIG RASFMILEKL PSNSHTEKVQ TPENVPRLFD LIKPKEARFA PAFYKAIRDT
LVADDMEQAN RIAFGGQRRW RVVTLAGQVI ETSGAMSGGG SQPMRGGMSS KLAADAVSPA
VLREFEKDSE TSAQQLQQAM EEARAAESEA DRLSRSGPEI DMALQKLNLD IENGKRRISE
AEKRVRDLKA QSKPNAGDIA RISELEKEIA SSTRALNQLE EKSGKITKEI QNLEKKILEI
GGSKLLTQKS KVDGIRLHIG LANDEITKAE VAKMKAEKDS AKLETTIENN KNAMEEVIKE
LEDLDSQLET LQEYVTALRE KVDTAKSAAE NSKEDLDNLR AELDEKEEHI SEFRQKEVEL
KQKLNDAEKE AKENLRLVEH WQDEHDKLKL EEIDDSDDED DEDEDDEEGR EPPADTPADP
DAMVKDEPGQ EPAAAPAAPE KKQKKKKRTE DLELHTYEED ELKRFKQREM VADAELLDEK
IKNAKPDLSV LREYKQRKAE YENREKDLQE TTSQRDAQKA TYDGLGKTRL DEFMAGFNLI
SLKLKEMYMM ITLGGNAQLE LVDSLDPFAE GIIFSVMPPK KSWKNISNLS GGEKTLSSLA
LVFALHVFKP TPLYFMDEID AALDFRNVSI VANYIKDRTK NAQFIIISLR NDMFELSHRL
IGIYKTANAT RSISIDNHAL LTAVSAPNPS SIVAVA
//