ID A0A074XKF6_AURPU Unreviewed; 1268 AA.
AC A0A074XKF6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=M438DRAFT_390933 {ECO:0000313|EMBL:KEQ85998.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ85998.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ85998.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ85998.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584979; KEQ85998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XKF6; -.
DR STRING; 1043002.A0A074XKF6; -.
DR HOGENOM; CLU_001042_0_1_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000030706; 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; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000030706}.
FT DOMAIN 552..668
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 78..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 433..495
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 738..790
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 828..964
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1063..1104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 144158 MW; E89E54FD9DF66D20 CRC64;
MGKLIRLELF NFKSYKGHHV LLFGDSYFTS IIGPNGSGKS NSMDAISFVL GIKSSHLRST
HLRDLVYRGR VLKTSRINAD GTATEVPEGE TQEPEAESGA QEEDQDTQTS TQRADPTNAW
VMAVYEDDAG DEQAWKRSIT STGQSEYRIN NRPVSAKQYN EALEAENILI KARNFLVFQG
DVEAIASQSS KDLTRLIEQI SGSLEHKADY DRLKIEAEKA AEDQAFRLNQ RRGINSEIKQ
YQEQKREVDN YTRKADERDQ AIVTHVLWKL FHFQQVVESS GAEIQKHQEE LKEHRRNVES
FEARLAEAQQ EQARAGREVH KLERNIKNKE KAVEEKENDL LPINEKITLS NKKLEVSRKR
IAEISKERDA QSRNADQLKK DLDVVQKAQS RWEQEWSAAQ QQAGRELSEA DLQEYNRLRG
DVNKRTAADQ IKVDNITRQL KTDEETVESL KSKVDSTENH ISKLDSEVAS LRSRRDELSS
TIRSINNEAD GKKKEFNTLT SERLKSAQKH TEIEEKLNEV LHKLNDASVS QRESEKEIRA
RETVAAMKRI FPGVRGQLWS LCKPKQKKYN VAVSTVLGRH NDSIVVDTEK VAKECIQYLR
DQRAGQATFI PLDTIMHKAP NANLKGMHRG MRLAIDTIDY ENAVERAISF ACGNSIVCDD
LQIARHLCYE KHVEAKAVTL DGTIIHKGGL MTGGNGSNDQ RNARKWEDSE VENLRRLKDK
LLADLGALPK GHRRQAEEET LQGELAGLES RRAFADEELK ALESNIESKR RELKHARHQL
EETRPKYEEQ AHGVTTLRSQ LESYSSSVAT VEDEVFAAFC QRLGYSDIRA YEAQQGSAQQ
EAAQKKLEFT TQRSRLENQL AFETQRLQTT KDRIAKLQAD VKEAQANIAN LESERDSLNN
ELDELNAEVE QMNEQLITRR TKYDEKSDKV AEHRREVAKR SKNIENTNKD ITALQEEVQR
SNSDRYSLLR KCRIEEINVP LTPQSRKLES LPLDGGMAAD EDAMDVDEEE GSQRVPEVND
YGIDLDFSEL DDDLKEDNSE QCETNLQETI STIQADLDKM APNMRAIERL EGVEARLKST
DDEFEASRKA AKEAKDQFDE VRETRSELFT KAYDHISGQI DQVYKELTRT ASFPLGGQAY
LDLEDTDEPY LSGIKYHAMP PLKRFRDMEH LSGGEKTMAA LALLFAIHTY APSPFFVLDE
VDAALDNANT ARLANYVKEH AGPGMQFVVI SLKTGLFQNS ETLVGVMRDQ TVNSSRTLTM
DLRKYQAA
//
