ID A0A168BZY1_CORDF Unreviewed; 1499 AA.
AC A0A168BZY1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=LEL_09351 {ECO:0000313|EMBL:OAA70760.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA70760.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA70760.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA70760.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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:OAA70760.1}.
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DR EMBL; AZHF01000009; OAA70760.1; -; Genomic_DNA.
DR STRING; 1081108.A0A168BZY1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000076881; 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:0051276; P:chromosome organization; IEA:InterPro.
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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; 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.
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|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 754..867
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..607
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 633..709
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 956..1148
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1264..1325
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 167747 MW; A58FF72CBAAD697D CRC64;
MSAAPKRSSR RVATRRNAVV DSDDDLSGIS KTQDDEPDEL DQEISQLPSR RTRSGRASMA
PTTTAKPKVT RTTRKTSAPV QKAKAEPEPT PEPEEKPAPE AEPEQDENAP VESAGDPVKT
EPAPSEPPKL SRRSATPRTS VTEVPKLAPQ TPSSKPLSPQ IGAPNVSPLA DITGMNTRLP
DVTQSVKPMR SMDTFLDKPL DIVVKQRTMA IPFVEDTTPK SRIVITYLML TNFKSYAGRQ
EVGPFHATFS SVVGPNGSGK SNVIDSLLFV FGFRASKMRQ GKISALIHNS AQYPDLDHCE
VAVHFQEVMD QPGGGHVVIP DSELIISRKA FKNNSSKYYI NNKTSDFTTV TTLLKDKGVD
LDHKRFLILQ GEVESIAQMK AKAANEHEDG LLEYLEDIIG TSKYKTPIEE SATEVESLND
ICVEKSSRVQ HVEKEKSSLE GKKDIALAFI RDENELTIKQ SALYQLFLHE CNENITVTEE
AISQMQAQLD DELEKHQGNE TLIKDLQRQY KQGSKEVDTQ DKETQALSKE MAQFDQERVK
FDEKKKFLDD KRKKFERTIA NAQKDSATAD ETIAESSKTM EKSTKDVADL ESQIEAEEAR
LINIREGLQG KTQKFSDQIA AKQKTLEPWL EKINEKQSSI AVAESELTIL QDKENAGAVA
LQELETKIKT IEGTKLEKAK ELKECQAQKS KLAKEAEKMQ SEIDILAEQE PKIRAKISST
RQKADEARSS LSSTQTRGNV LAALMRMRES GRIEGFHGRL GNLGTIDEKY DVAVSTACGA
LDNFVTETVE SGQQCIEYLR KNNLGRGNFI CLDKLKDRSL APIQTPENAP RLFDLVKPQH
DRFRPAFYHA MQDTLVAVDL AQANRIAYGA KRWRVVTVAG ELIDKSGTMS GGGTTVKKGL
MSSKLSSDIT KEQVAKLEQD RDTWETKFQE FQEYQRECEN RMREINDEIP ALDTKMQKIG
LEVESATRNI ADLQRHVKSV SQEYQPSVTD ASRIKELQKE IASLNSAVAK LRDETSSVEE
EIKALQDKIM EVGGEKLRMQ RALVDGLKDQ ITSHNEEISF AEVRKAKAEK QKVKLDKDTA
KASKERDAAV AELEKLDDDI SNQGTKADEL RQNVQDAKAA LATKKAQVQE MKEELDVKTS
ELNETRAVEI EMRNKLDENR KVLTENQKRL RYWDDKLSKL VLQDINDLIG ESAPKRATPA
PETNGEKSQV DSEDVEMSET EQAEKGDISM GDAEEPLAEE QERSLHQPQE LPQYTPDELA
EMSKETLKGE IAALEEKTQN VAIDLGVLAE YRRRVEEHAS RSSDLQSALD QRDSAKKRCD
DLRRMRLEGF MAGFSAISLR LKEMYQMITM GGNAELELVD SLDPFSEGIL FSVMPPKKSW
KNIGNLSGGE KTLSSLALVF ALHHYKPTPL YVMDEIDAAL DFRNVSIVAN YIKERTKNAQ
FIVISLRNNM FELAARLVGV YKVNHMTKSV TIENQDFIAR PQPQPRPAMG GHTTTLALR
//
