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Database: UniProt
Entry: A0A093IIN9_FULGA
LinkDB: A0A093IIN9_FULGA
Original site: A0A093IIN9_FULGA 
ID   A0A093IIN9_FULGA        Unreviewed;       977 AA.
AC   A0A093IIN9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Structural maintenance of chromosomes protein 4 {ECO:0000313|EMBL:KFV98623.1};
DE   Flags: Fragment;
GN   ORFNames=N327_07912 {ECO:0000313|EMBL:KFV98623.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFV98623.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFV98623.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFV98623.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   EMBL; KK588552; KFV98623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093IIN9; -.
DR   Proteomes; UP000053806; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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.
DR   SUPFAM; SSF57997; Tropomyosin; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053806}.
FT   DOMAIN          610..725
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          271..298
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          766..842
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          889..972
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         977
FT                   /evidence="ECO:0000313|EMBL:KFV98623.1"
SQ   SEQUENCE   977 AA;  111167 MW;  30A57DB1377BA73E CRC64;
     MPSKSTKTST AAHRKGREPL EGSTSDMEVE NEGDRQLSEV PPQAVSNEVL DNRSLEEILG
     SISPPPPPAM TNEAGAPRLM ITHIVNQNFK SYAGEQTLGP FHKRFSCIIG PNGSGKSNVI
     DSMLFVFGYR AQKIRSKKLS VLIHNSDEHT DIQSCSVEVH FQKIIDKEGD DYEVIPNSSF
     CVSRTAYRDN SSVYHINGKK KTFKDVGILL RSHGIDLDHN RFLILQGEVE QIAMMKPKGQ
     TEHDEGMLEY LEDLIGSARL KDPIQTLCRR VEILNEQRGE KLNRVKMVEK EKDALEADRN
     KAIEFLCLEN KMFKEKNNIC QYYIYDLKKR VNDMEMQKEK INEETKDVNE KSSKLADEMK
     TKNKALKELE KKLNKITTFV EENKEKFTQL DLQDVKIREN LKHAKSKAKK LEKQLQKDKE
     KVAELKNVPS SSEKAISEAT SKKELLEKTK EKEEEKLKQV MDSLKEETQG LQEEKESKEK
     ELMEFSKAVN EARSKMDVAQ SELDIYLSRH NTAVSQLNQA KEALMTTSET LKERKAAIKD
     IDVKLPQAEQ ELKEKDNDLE KLGREESGAK NLVRNLRQKV EEAKSSLALS RSRGKVLEAL
     LQQKKSGNIR GLYGRLGDLG AISEKYDVAI SSSCGALDNI VVDTIDTAQE CVNFLKATGI
     GVATFIALDK MAVWEKKIQK IPTPENTPRL FDLVKVEDEK VRLAFYFALR DTLVANNLEE
     ATRVAFQNDK RWRVVTLQGQ IIEQSGTMTG GGGKIMKGRM GSSVVMDVSE EEINKMESQL
     QKDSERAVQR EEEKLQLEEA IRKLRQDVRE MRNTLEKYTA SIQSLSEQEI HLKTQVKELE
     ANVIAAAPDK NKQKELEKIL STYKKDYDCI AEKAGKIENE VKRLHNLIIE INNHKLKAQQ
     DKLDKINKEI DECTSTITKA QVAVKTADRN LKKSEESVLR TEKEIEDNEK EIKNLTEELT
     TLEDKATEVI NDCRQAE
//
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