ID G1X6V0_ARTOA Unreviewed; 1434 AA.
AC G1X6V0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN ORFNames=AOL_s00054g594 {ECO:0000313|EMBL:EGX51218.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51218.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX51218.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EGX51218.1}.
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DR EMBL; ADOT01000088; EGX51218.1; -; Genomic_DNA.
DR RefSeq; XP_011120212.1; XM_011121910.1.
DR STRING; 756982.G1X6V0; -.
DR GeneID; 22891153; -.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; G1X6V0; -.
DR OMA; CPALDNM; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000008784; 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:UP000008784}.
FT DOMAIN 758..871
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..439
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 479..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 577..611
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 651..741
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 967..1180
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1217..1278
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 160699 MW; 5C8267FCF3136B43 CRC64;
MSGRSRRAAS RRVVVEESDN EEEQVQQEEE EEEEEEDQEE EETPPPPPPK KRGRPSRTST
SAPSPAKPPP KPRGRRKVAP DPEPKIEEVE EQIALATTED AMEFESTPAP ETIPTPVQVS
TPRQSVPRSS VPPADTIVLA SPARTQQILR TPIKRAPSHD VRAGSQTPQS PSVVKSPSVN
GNSSVNGDTG AATPTKAEPQ SQVPPQATPK PRIPTPPPPE PVGPKARIVI THLVMINFKS
YAGRQEVGPF HSSFTSVVGP NGSGKSNVID SLLFVFGFRA SKMRQGKLSA LIHNSAGHPN
LEFCEVEVHF QEVIDLPTGT EIIPDSTLII SRKAFRNNSS NYYINGKTSN YKIVTSLLKD
RGVDLDHKRF LILQGEVESI AQMKPKAQGE HDDGLLEYLE DIIGTSNYKQ PIEESAAEVE
KLNEVCQEKQ SRVQLVQKEK DGLEAPKNAA VAYINNENEL AMKQGALYQV YMSDCENVIA
VTEDSMNQMQ ISLQEEQDKH QGKEEEVKGL EKDYKRGVKE FEDVEKKTAA MVKEAAKFEK
DTVKFEEQKK FLVNKQKKTE KTLNSSRLAG SEQVGLVQRY TDDVNRNTAE IVELENRKKQ
EELVLQQIRD ELAHKTQGLS EQISVKEAAI QPWKEKVVSK ENEIAVIQSK LDILHERANA
GQKAVEEAEA KIISIQQAYE VIDAGFKTGQ KQGRAIMRDI KRLEEEYAEF QKQEPDIKAA
LSNSRQKADE AKASLAATQN QGNVLSGLMR LKETGRIEGF HGRLGNLGAI DAKYDVAITT
ACPALENMVV DTVDVGEQCI AHLRKNNLGR AKFILLDRLA KRDLGPIQTP ENVPRLFDLV
TPKLDAYKPA FYSVLQDTLV ANDLTQANRI AYGARRWRVV TLDGQLIDKS GTMSGGGNRV
SKGGMSSKLV ASTTQATVTK LEAERETQEQ TWSEFQKQLR AIEDALRENR DQVPKMETQL
KKQQMELEAK KQLGMDAQRR LEELKLENKP SSSHHGEIRA FEKEIAVLQN HITKLNSETA
GAEAEIKTLQ DKIMEIGGIR LRSQKTLVDG IKEKIDTLNE EMTVAEASRV KAEKARQKNE
KAEMNATKEL ESVERDLGKL TEEMNSHAWK AREAMKAAEA QKDFTDDCKE KLAELKAQLD
EKASDISEAR SKEISMKNTL EQHEKALADN RKRYAHWREK FSKLSLQSLA EIEGEEMPDA
PNQIPVYSTD ELADMDKEKL KAEIVILEEK LQNVNVELGV LQEYKRRVAE YNERSGDLNA
AVAERDAVKK RCDDLRKRRL DEFMEGFSTI SLRLKEMYQM ITMGGNAELE LVDSLDPFSE
GILFSVMPPK KSWKNISNLS GGEKTLSSLA LVFALHHYKP TPLYVMDEID AALDFRNVSI
VASYIKERTK NAQFIVISLR NNMFELASRL VGVYKVSQMT KSVTIENQDF MVRN
//
