ID W2SBF4_9EURO Unreviewed; 1177 AA.
AC W2SBF4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 13-SEP-2023, entry version 44.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=HMPREF1541_00215 {ECO:0000313|EMBL:ETN46032.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN46032.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN46032.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN46032.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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. SMC2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005231}.
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DR EMBL; KB822711; ETN46032.1; -; Genomic_DNA.
DR RefSeq; XP_008710744.1; XM_008712522.1.
DR AlphaFoldDB; W2SBF4; -.
DR STRING; 1220924.W2SBF4; -.
DR GeneID; 19967554; -.
DR VEuPathDB; FungiDB:HMPREF1541_00215; -.
DR eggNOG; KOG0933; Eukaryota.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; W2SBF4; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000030752; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR CDD; cd03273; ABC_SMC2_euk; 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; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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.
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 DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT DOMAIN 521..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 937..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..294
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 326..381
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 438..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 683..904
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1177 AA; 131168 MW; 8E5E6B4B8FCEF5DC CRC64;
MRIVELIIDG FKSYQVRTVI SGWDDSFNAV TGLNGSGKSN ILDSIAFVLG INNMSTVRAQ
NLQDLIYKRG QAGVTKASVT IVFDNGDKNK SPIGFEEYAQ ISVTRQIVMG GTSKYLINGH
RAQQQTVQNL FQSVGLNINN PNFIIMQGRI TKVLNMKSVE ILAMIEEAAG TRMFEDRKDK
ANKTMAKKEM KVKEIEGLLK EEIEPKLDKL RGEKRAWLDY QKTQGELERL TRVVVAAEYV
RGGEKMRQAT DEHEAKRAKM QHLEDNAVKL KREIENLEED AQRVRAVREK EMRKGGRFQA
LENQVKEHSH ELVRLATVLD LKKSSLSEEE SRKKDVAKSV KALEKQVAEK KAAFEKLQAN
YDSSKAEVDA QNAEMESKEE LLSTLQTGVA SREGQESGYQ GQLQEARNRV TSAGTEQEQA
KLKISHLEKQ IKEDEPRAQK AKNQNAGLIN GLDSLRKQAA KLEADLSKMG FEPGREEAMQ
ERQTTLQKTI RKLKEEADGL KRKVANVDFN YSDPSPNFDR SKVKGLVAQL FTLDKDKSMA
GTALEICAGG RLYNVVVDSA ETGTQLLQKG KLKKRVTIIP LNKISAFRAS AEKVGAAQKL
APGKVDLALS LIGYDYEVSA AMDFVFGTTL ICQDAETAKK VTFDPSVRLK SVTLEGDVYD
PSGTLSGGSS PNSSGVLVIL QKLNEVTKNM MQHQQELDTL RQQMQSEQQK LASIRAVKQE
LDLKSHEIKL TEEQIKGNSS SSIIAAVEEM KESIVQLKQA MADAKTTQAE AQKDVKRIEK
DMVDFNRNKD SKLKELEKSL ADLKKNLSKT TVAIKTMQKE LQEARLDSEQ AVSDLAAAEE
QLAEVEGGIS AQNEELASLR EEEAAAKSAH DVAQAELQEE QAKLTSFDNE LQELESAKSR
KSKQVTEESL EAQKLSHAVE KLAKDSAAAA SHVASLEKEH DWIHDTKDQF GKPNTPYDFH
GKNLAESRAI MKNLTERFQG MKKKINPKVM PMIDSVEKKE AGLKNMLRTV VRDKKKIEET
IITIEEYKKE ALLQTWRKVT EDFGNIFADL LPGNNSAKLE PIDGDVSRIG EGLEVKVMLG
KVWKTGLAEL SGGQRSLIAL SLILALLQFK PAPMYILDEV DAALDLSHTQ NIGRLIKTRF
MGSQFIVVSL KDGMFQNANR VFRTRFSEGT SVVSVMQ
//
