ID A0A2B7X973_9EURO Unreviewed; 1281 AA.
AC A0A2B7X973;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=GX51_02973 {ECO:0000313|EMBL:PGH05449.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH05449.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH05449.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH05449.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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}.
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:PGH05449.1}.
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DR EMBL; PDNC01000030; PGH05449.1; -; Genomic_DNA.
DR STRING; 2060905.A0A2B7X973; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000224080; 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; 1.20.1060.20; -; 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; 2.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000224080}.
FT DOMAIN 545..661
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 77..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..318
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 354..388
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 412..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 737..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 866..939
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1057..1098
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 145834 MW; 13122F07D9DADD23 CRC64;
MGKLIRLELF NFKSYKGHHT LLFGDAFFTS IIGPNGSGKS NSMDAISFVL GIKSSHLRST
NLRDLVYRGR VLRTSTINDD GSASKNPQNG VNGGGDVEPS QEPAERNDPK VAWVMAVYED
DAGEEQHWKR SITSQGVSEY RINNRIVTAQ QYNQSLEDEN ILIKARNFLV FQGDVESIAS
QSPRDLTRLI EQISGSLEYK AEYERLKAEQ EETAEIQNAQ LNRRRGINSE IKQYQEQKRE
AENYARKADE RDQAIITHIL WKLFHFQRLI EESSAEIQKH QDELKEFRRG VEKYEKNLEE
AKKDHARAGR NVAKVEKSIS SKRKDIEDTT NSLVPVDEKI EISKQKVVRY ATRISEIEKE
SNAQSKTVKQ LEKDLKVVEK AQSQWEDEWK KTASKRGIQL SDSDLHEYNK LKEDVNKRSS
AAQIKLANLK RQRKADAETV NSLKSNFEST EWQVKNLQSD VNNMLDRKSS MAETIEATSK
EISQKKKELN NLTSERLRVA QMRTELEEKL QVTLKKLLEA DDGRKQSEKE LRTKELISTL
KRIFPGVKGR VSELCKPKQK KYQDAVSTVL GRHFDSIVVD NEKTAKECIQ HLRDQRAGQA
TFIPLETIQV KAFNSSLKGM HRGMRPAIET VDYDNSVSRA ITYACGNAIV CDDLATAKYL
CYERGVDAKA VTLDGTVIHK GGLMTGGRGP GHQQSKRWED TDITNLHKLK DKLIADLGNL
PKAHRKGAEE ESLQGQLAGL EQRLAYSRDE LKALDRNIES RSSEVEFSKR QMKSVQPKYL
QKKRALEELD ESIEEAQSSV SGVEDEVYQA FCRRLGYSNI REYEAQQGSL QQEAAEKKLE
FTTQKSKIEN QLSFEKQRLQ ATDDRIEGLR SQAERDRVLI AELEAERKTI KDRLDTLNAE
LELLGEDLAE QKEAYSQSAE NLAAQRQEVQ KRSRNVEATL KAISSLDGER QRYASGRYAL
LRRCKLEDID IPLEKGSAPL STLPIDDLVQ NDEDAMDVDE DPNVGSIQAS TIHDYGIEVA
FESLGDSLKE DSDDKIEEEL QDRIRSLNSE LDKMAPNMRA MERLEGVENK LRSTEKDFED
ARKRARKAKE DFEAVMRKRS ELFNKAFTHI SEQIEPIYRD LTKTASYPMG GKAYLDIEDS
EEPYLDGIKY HAMPPLKRFR DMEHLSGGEK TMAALALLFA VHSYQPSPFF VLDEVDAALD
NTNVARVANY IRDHAAPGMQ FIVISLKTGL FQNSEALVGI YRDQAANSSK CLTLDVRLFT
MKTFIIRCLL FVHHSLIALV N
//
