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Database: UniProt
Entry: A0A1Y2GHM2_9FUNG
LinkDB: A0A1Y2GHM2_9FUNG
Original site: A0A1Y2GHM2_9FUNG 
ID   A0A1Y2GHM2_9FUNG        Unreviewed;       948 AA.
AC   A0A1Y2GHM2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN   ORFNames=BCR41DRAFT_110256 {ECO:0000313|EMBL:ORZ11270.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ11270.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ11270.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ11270.1,
RC   ECO:0000313|Proteomes:UP000193648};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
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:ORZ11270.1}.
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DR   EMBL; MCFF01000028; ORZ11270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2GHM2; -.
DR   STRING; 64571.A0A1Y2GHM2; -.
DR   InParanoid; A0A1Y2GHM2; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000193648; 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: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; 1.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193648}.
FT   DOMAIN          521..642
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          253..280
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          326..381
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          410..472
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          676..932
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   948 AA;  107426 MW;  310A74A6FDB53A36 CRC64;
     MRIEELIIDG FKSYATRTSI TGWDPEFNAI TGLNGSGKSN ILDAICFVLG ITNWSQVRAS
     SIQDLIYKRG QAGVTKASVT VVFNNQDREQ SPVGFESSKQ ITITRQILIG GRSKFLVNGH
     TAQQQVVQTL FQSVQLNINN PHFLIMQGKI TKVLNMKPPE ILSMIEEAAG TRMFEERKDK
     ALKTMAKKEK KVAEITQLLA EEIIPKLDKL RAEKRAYLEF QKTQTEIERL SRIVVSFDYS
     RYEQRYSKSK HDLETKLALI DQKSAEIEQL QSAISNIAQH IETITANRLK EMTQGGKFQT
     LDATVKDLSK EIVKVKTQRD LKDKEAQEEE QNHSGLLSTL KETEKTLHEK RVEFEKLQVT
     YNDLRRKHDE QQEQVRMNEE LIQTLSTGLA AEEGHENGYM EQLQRVKASA AQATTLVDQS
     RLKLKHLETE LSEKRKQASL AQKNNKDLSA GLSAAKQQVK QLEETLHRQS FDPEQERALQ
     MEKAAQSDAI AKLSEKIETT SRKVAGLDFQ YSNPTPNFDR TSVKGLVAEL FTVLPEHANA
     ATALEICAGG RLYNVVVDNE IVGSQLLQNG KLRKRVTIIP LNKITAFRAH AQKIATAQRL
     APEKVNLALT LIGYEDQLET AMAYVFGNTL ICADADSAKK VTFHQEVRMK SVTLEGDVYD
     PSGTLQGGSR PTGGGILASL QEIHALKNQL NEHRQQLQKI NQQLSNISQA ARAYAELKQK
     IELKTHELRL CEQQLSGSEH VQLMEQTERL EKEIKALRAG IEDGNHKKAE AVKRCQEIEK
     EMKDFKKNKD GKLHELMQKL AKSKAELTKN APRVKAMQRE HQTFVLELEQ LEKDVKGASQ
     ELSESKSVIS KFKDERDRLQ EQLVMLESSL EKTQLEFERE KAQLNAYDEE LKELEALSKQ
     KAKVVAESRL EIQNLTHETD RLSKENNSLL NAINDLEGSH DWIHDQKL
//
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