ID E4V2R0_ARTGP Unreviewed; 1289 AA.
AC E4V2R0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=MGYG_06616 {ECO:0000313|EMBL:EFR03622.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989827; EFR03622.1; -; Genomic_DNA.
DR RefSeq; XP_003170630.1; XM_003170582.1.
DR STRING; 535722.E4V2R0; -.
DR GeneID; 10025871; -.
DR VEuPathDB; FungiDB:MGYG_06616; -.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_1_1; -.
DR InParanoid; E4V2R0; -.
DR OMA; SYIRDHT; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000002669; 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:UP000002669}.
FT DOMAIN 545..661
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 78..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..388
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 412..495
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 737..942
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1057..1091
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1289 AA; 146570 MW; 8F912678BA0DD0A9 CRC64;
MGKLIRLELF NFKSYKGHHT LLFGDAYFTS IIGPNGSGKS NSMDAISFVL GIKSSHLRST
HLRDLVYRGR VLRTAKINDD GSASKDPAAG QSEGQNGDVA DEPAERNDPK SAWVMAVYED
DAGEEQQWKR SITSQGVSEY RINNRVVTAQ QYNDALEAEN ILIKARNFLV FQGDVESIAS
QSPKDLTRLI EQISGSLESK ADYERLKAEQ EEAAEHLNFQ LNRRRGINSE IKQYQEQKRE
AETYARKAEE RDQAIITHIL WKLFHFQRLI VESSAEIQKY QDELKEFRRG VEKYEKNLED
AKVEHARVGR DVSRAEKGIK LKEKEIEEAT NSLVPVNEKI EITGKKVAKY AARVDEVSKE
ALAQSKTVKQ LEKDLKIVEK AQGQWENEWK QTIAVKGIQL TDADMQEYSR LKEEVSKRSS
STQLKLDNLK RQRKADAEAV NNMKSNLESV EWQAKNLQTD MDHILERKSV IAATIKSTTK
EIDATKKELN SLTSERLRVA QMRTELEEKL QVTLKKLLEA DDGRQQSEKE QRTKEMIATL
KRIFPGVKGR ISELCQPKQK KYAEAVSTVL GRHFDAIVVD NEKTAKECIQ HLRDQRAGQA
TFIPLETIQV KPLNSNLKGM HRAMRPAIET VDFDSSVSRA ITYACGNSIV CDDLATAKYL
CYEKGVEAKA VTLDGTVIHK GGLMTGGRGP GQRNAKRWED TEVANLNKLK DKLMADLANL
PKAHRRGSEE ESLQGQLTGL EQRLAYSKDE LSALEKNLES KSSEVDFAKR QMKSVQPKYR
EKSALLESLD QSIEDIQSSV TEVEDKVYRD FCKRLGYKNI QEYDAQQGSL QEEAAEKKLQ
FTTQKTKIEN QLSFEKQRLQ ATEIRIDSLR TQSQKDESMI AELEAERGSI QERLDELNEE
LASLNDKLQD QQNLFSESSE NLAQQRRELQ RRSKNVEAAL KTISGLEADV QRHSSGRYTL
IRRCKLEDIN IPLTADSEPL DKLPIDELVQ PDPDAMEIDE DSNNVVSQNH FVQDFGIEVD
FSSLGDSLKE ESDDKLEEEL QERVRSLNNE LDKMAPNMRA IERLEGVESK LRTIEKDFED
SRKRARKAKD DFEEVMQRRS ELFNKAFTHI SEQIEPIYRD LTRTESYPMG GKAYLDIEDS
EEPYLDGIKY HAMPPLKRFR DMEHLSGGEK TMAALALLFA IHSYQPSPFF VLDEVDAALD
NANVSRIANY IRDHAAPGMQ FIVISLKTGL FQVSEALVGI YRDQAANSSK ALTLDVSLVI
SPDYESPCLT LYSYANTGDP KRHSFPRPC
//
