ID   A0A1B8G1B1_9PEZI        Unreviewed;      1353 AA.
AC   A0A1B8G1B1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=VE02_01831 {ECO:0000313|EMBL:OBT89633.1};
OS   Pseudogymnoascus sp. 03VT05.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT89633.1};
RN   [1] {ECO:0000313|EMBL:OBT89633.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03VT05 {ECO:0000313|EMBL:OBT89633.1};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-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. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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DR   EMBL; KV459367; OBT89633.1; -; Genomic_DNA.
DR   Proteomes; UP000091872; 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; 1.10.287.1490; -; 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; 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}.
FT   DOMAIN          647..762
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          176..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          528..611
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          798..953
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          989..1051
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1155..1189
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1353 AA;  152923 MW;  ABBCBF636DEC5568 CRC64;
     MGEAEKNTSR DTCRVGGLED VSREPRLIAT ARATVSINVN ESDSFSGSFV KAARFDSSET
     HTGSTKSISK LKNTYACFFT SCTYLIDTTS PRKAQLSKMG KLIRLELFNF KSYKGHHTLL
     FGDSYFTSII GPNGSGKSNS MDAISFVLGI KSSHLRSTHL RDLVYRGRVL KTSKINDDGS
     ADAPAANGDA NGDVNSDGEG ADLQISERND PKSAWVMAVY EDDAGDELKW KRTITNQGAS
     EYRINNKVVT AQHYNDALEA ENILIKARNF LVFQGDVEAI ASQSPKDLTR LIEQISGSLE
     HKAEYERLET EAQEAAENQN NSLQRRRGIN SEIKQYQDQK KEADNFQAKA DERDDAIVKH
     ILWKLYHFQK VIDESSEEIA KHQEELKKFR HGIRKYEAEL DEARKEHART QKEVGKVERG
     IKSKERDVED KMNSLVPIDE KVEHVQRETA KVEKRINDLT KERDSQLAGI QSAKKELALV
     DKAHKLFETQ WKEQMKKQGK ELSSDDLKEY NKLKAQVINQ SSSNQAKLDN LLRQLKTDEI
     TVNSLKSKVQ SSQSQVEKLG QEASQITERR DAMKVSLKQI TKDIDGKKKE YNVLQSERLR
     VNQKRTEIEE KIEDVVKKLD FANDGRRQND REARTKEIVT SLKRIYPGVR GRIGELCKPK
     QKKFDEAVIT ALGRDFDSVV VDTEKTGTEC VQYLKDQRRP PMTFIPLDNI KVNAVNSNLK
     GLSKARLTID TIDFDSTLER AMSYACGNSI VCDDLATAKQ ICYDKGMQVK AVTLEGFVIH
     KAGLMTGGRG AEGKGGKRRF EEQDVQNLEK MLEKMKTELD SLPKANRRGA AEETLQSDLS
     GLEQRLAYTK SELAAFEQNL ASKKKELDYE KRQLSDIQPK YKEQAASLET LQESVQNFKD
     AVSKVEDKVF AGFCQRLGYD NIRDYEVQQG TLEQEAAQKR NDFELQKQKL TSRLTWETSR
     VDDTKARLKR LEDQTFSLSQ DIDTYNSSKE KLEESLDVDN AEIEVLKEQL TEAKQKSSKK
     NEKVVQARDE LQKRSKNVDT VQRAISSLES EAQRAAAGRY AQLRRCKLEQ IRIPLADGSS
     DLESLPVDNM PDVDPDAMDV DDGDAVDPVL INDGIQIDFD ELDEDLTESG EEHIEETLLS
     QIAALNAALE KLNPNMRAID RLEAVEARLK TTEQDYEDAR KTARDSRDAF LEVKEKRFNL
     FNKAFSHISE QISHVYKDLT RSAAYPLGGQ AYLDIEDSDA PYLSGIKYHA MPPLKRFRDM
     EHLSGGEKTM AALALLFAVH SYQPSPFFVL DEVDAALDNA NVEKIRNYIR EHANPGMQFI
     VISLKTGLFQ GSESLVGVYR DQDANSSNTL TLD
//