ID   A0A1X2IK22_9FUNG        Unreviewed;      1201 AA.
AC   A0A1X2IK22;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=BCR42DRAFT_325683 {ECO:0000313|EMBL:ORZ17904.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ17904.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ17904.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ17904.1,
RC   ECO:0000313|Proteomes:UP000193560};
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       ECO:0000256|PIRNR:PIRNR005719}.
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:ORZ17904.1}.
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DR   EMBL; MCGE01000009; ORZ17904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2IK22; -.
DR   STRING; 90262.A0A1X2IK22; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000193560; 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:0051276; P:chromosome organization; IEA:InterPro.
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; 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   PIRSF; PIRSF005719; SMC; 2.
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   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT   DOMAIN          471..584
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1155..1201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          183..277
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          320..375
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          634..741
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          785..883
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          955..992
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1172..1201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1201 AA;  136872 MW;  A06B70181F1E1C17 CRC64;
     MILNNFKSYA VVGPNGSGKS NVIDALLFVF GYRANKMRQG KLSELIHNSA QHPNLESCSV
     EVHFQEIIDS DKQVGQYDTV PNSRLVVSRQ ASRNNSSKYF INERSSNYMD VTTLLRGRGI
     DLDHKRFLIL QGEVESIALM KPKAKDGNDD GLLEYLEDII GTSKYKDAIV DANTRLEEFN
     VVRAEKLNRV KFVAKEKENL EDKKLEAENY LENENELSKR KNELYQVYRY EAQGNMEVAE
     KAVTELKEKL KLDEEKNAKV EEEIKAFKTA YQDEVKQYNS LEADYSKIMK RHATFEKDDV
     ELRAKKEHLQ KRQDKGKETI ESEREALTKA EDTIKKNTQE IDKRQKDLKA SEKQLKQEEK
     NLDEINRDLQ GKTAGFMADI EEQQTQLAPW TEKINDKKKA INLKNSESEI LSKRIASGAE
     ADLGERETSC RKEVSTARQK HDEAKSTMQQ SQSRGKVLDG LLRMRDTGRI KGIYDRMGNL
     GVIDDKYDVA ISTACPALDN IVVETVEAGQ ACIEYLRKNN LGRAVFTVLE KQQQQNMSSI
     ETPDNVPRLF DLVQPKDDKF APAFYSVLRD TLVANDLHQA NRIAFGGKKR WRVVTMDGKL
     IEKSGAMTGG GNRQLRGAMG AQFQNEDDVD PEMVATLEKE RNDLEMEFRK LVEEKRALEL
     VLRAKQASLP KKQMVLEKLQ LDVRSLDSQL EDDNRRLEEL KAHSEPKPQD VQRVEEIKHE
     VEQLTVELTE LNEKTATIQA TIDGLHEEIM DVGGMDLRLQ KIVVDDVRKR IDLHNDKITK
     CSVHKTKAEK DVIKIEANIK KTEADLENLL SESAELDRQL IANTTAAASL LADAEDMKKA
     SQATKKEAMD TMKQELDTKS ESINESRKAR LEITNQLEDY QKTYTDNKRK AEHWSDQQSR
     LTMHKLWNEK GDETILPIYT IEKVREFQQD KQVIKGEIAE IEAFVQSAKP NLSVLEEYRR
     REEEYKDRAT DLESITKKRD QVKYEADDLR KKRLDEFMQG FNIISQKLKE MYQMITLGGN
     AELELVDSLD PFSEGIVFSV MPPKKSWKNI SNLSGGEKTL SSLALVFALH HFKPTPLYVM
     DEIDAALDFR NVSIVANYIA ERTKNAQFVI ISLRNNMFEL ADRLVGIYKT SNCTKSIAIN
     PSMVATFSAL TNIDNNNGDD DGNKRQSTPS GDRHSSRSQS RAPSSTPVPS TMTDPISTSP
     V
//