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Database: UniProt
Entry: A0A1L7XGN4_9HELO
LinkDB: A0A1L7XGN4_9HELO
Original site: A0A1L7XGN4_9HELO 
ID   A0A1L7XGN4_9HELO        Unreviewed;      1415 AA.
AC   A0A1L7XGN4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=PAC_14107 {ECO:0000313|EMBL:CZR64209.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR64209.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR64209.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR64209.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   EMBL; FJOG01000026; CZR64209.1; -; Genomic_DNA.
DR   STRING; 576137.A0A1L7XGN4; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000184330; 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; -; 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; 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; SSF90257; Myosin rod fragments; 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:UP000184330}.
FT   DOMAIN          741..854
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          490..524
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          553..594
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          894..1145
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1197..1258
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        72..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1415 AA;  157898 MW;  D200C29E2D9EF2E4 CRC64;
     MSESPIRPSR RAAARRKVVV DSDEEEEQVT PKMEEDSGED FTPAPKKSPR KAAAGRRKTT
     NAVAATPRTG DRARKSVAKE NIEPSEMFDP EQTVQPEPES PTKKASPRKR KSAPVRASRV
     SGTPELAPPL PTPQASQSPE PSEQHCTPLA DITLTINERP STSGSQSSQS SVVKPINAMD
     TILEKPMDIV LKSRTMAAPV VEDTGPKPRI VITYLILTNF KSYAGRQEVG PFHASFSSVV
     GPNGSGKSNV IDSLLFVFGF RASKMRQGKI SALIHNSATH PDLDHCEVAV HFQEVMDQSN
     GPPQIIPNSD LVISRRAFKN NSSKYYLNGK ESNFTVVTTL LRDRGVDLDH KRFLILQGEV
     ESIAQMKPKA ASEHDDGLLE YLEDIIGTSK YKTPIEESAK EVETLNEVCV EKSGRVQHVE
     REKNGLEDKK NKALAYIKDE NELTVKQSGL YQLYINECGD NISVTEEAIG QMQAQLDAEL
     EKHQGNEDGI KQLEKQYKKG QKEYETLEKE TQSILKEMAK FDQEHVKFEE KRKFLTGKQK
     KLEKTISSSE TAAIDAQATI EECTAEIEKS AEEIAAMEKR MKAEEKELVS IRENLKGKAQ
     AFSDQIAAKQ KSLEPWNEKI NQKQSAIAVA ESELTILHEK ANAGAVALEE TEAKIASIEE
     GREAKLAELE QCKADRAKLE KEAVKVEKEL NSLSKNEPEL RSRLSGARQK ADEARASLSN
     TQSQGNVLAG LMRLKESGRI DGFHGRLGNL GTIDQMYDIA ISTACGALDN FVTDTVEGGQ
     QCIEYLRKTN LGRGNFMCLD KLGSKDLSPI DTPENVPRLF DLIKAKDEKF RPAFFHSLQN
     TLVATDLAQA NRIAYGAKRW RVVTLDGQLI DKSGTMSGGG NTVKKGLMSS KLVADTSKEQ
     VAKLEVDRDA LEQDFQKFQE RQKELEFSLR DLKDQIPRLD TKMQKIGLEV ESSARNLADA
     QRRIKELSKE HQPSKTDDSR VASLEKEIAK LNKEIEKLHG ETASVEQEIK ELQDKIMEVG
     GDKLRTQKAK VDALKEEIAN VNEAISTAEV TRAKAEKSKT KQEKDHAKAT KELQAAISDL
     ESLEEDIKNQ SANAEGYQAR VDEAQEALKA KKSNLSTLKS ELDEKTAALN EIRAIEIEMR
     NKLEENQKVL VENQKRLKYW HEKLGKLALQ NISDLGEETE AQDLPTYTKD ELADMSKDTL
     KSEIAALEEK TQNVNVELGV LAEYRRRVEE HAARNADLQS AVSQRDTAKK RCDDLRRLRL
     EGFMEGFSTI SLRLKEMYQM ITMGGNAELE LVDSLDPFSE GILFSVMPPK KSWKNISNLS
     GGEKTLSSLA LVFALHHYKP TPLYVMDEID AALDFRNVSI VASYIKERTK NAQFIVISLR
     NNMFELASRL VGVYKVNHMT KSVTIENRDY IHGTA
//
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