ID   A0A1S2ZT14_ERIEU        Unreviewed;      1285 AA.
AC   A0A1S2ZT14;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=SMC4 {ECO:0000313|RefSeq:XP_007524121.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007524121.1};
RN   [1] {ECO:0000313|RefSeq:XP_007524121.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   RefSeq; XP_007524121.1; XM_007524059.1.
DR   STRING; 9365.ENSEEUP00000012326; -.
DR   CTD; 10051; -.
DR   eggNOG; KOG0996; Eukaryota.
DR   InParanoid; A0A1S2ZT14; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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; 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.
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   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT   DOMAIN          611..726
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          367..573
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          767..843
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          868..1008
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1285 AA;  147066 MW;  3E526BE0307FE7EE CRC64;
     MQRRGAPTST ARRAPDPPRS PAGADDDVEP EPAATGGEYP ATNLETPSEE IDNRSLEEIL
     NSIPPPPPPA MTNEAGAPRL MITHIVNQNF KSYAGEKILG PFHKRFSCII GPNGSGKSNV
     IDSMLFVFGY RAQKIRSKKL SVLIHNSDEH KDIQSCTVEV HFQKIIDKEG DDYEVIPNSN
     FYVSRTAYRD NTSVYHISGK KKTFKDVGNL LRSHGIDLDH NRFLILQGEV EQIAMMKPKG
     QTEHDEGMLE YLEDIIGCGR LNEPIKVLCR RVEILNEHRG EKLNRVKMVE KEKDALEGEK
     NIAIEFLTLE NEIFNKKNHL CQYYIYDLQK RIANMEAQKK IIHEDTKEIN QKSNILSNEM
     KTKNKAVKDV EKKLNKITKY IEENKEKFTQ LDLEDVQVRE KLKHATSKAK KLEKQLQKDK
     EKVEEFKSLP AISEKTITET TARSNTLEKE KEKEEEKLKE VMDSLKQETQ GLQKEKESRE
     KELMGFSKSV NEARSKMDVA QSELDIYLSR HNTAVSQLTK AKEALTAASE TLKERKTAIE
     DIEAKLPQTE KELKEKEKEL QKLTQEEINF KNLVRDLFQK VEEAKSSLAM NRSRGKVLDA
     IIQEKNSGRI PGIYGRLGDL GAIDEKYDVA ISSCCHALDY IVVDSIDTAQ ECVNFLKSQN
     IGVATFIGLD KMAVWAKKMA KIQTPENTPR LFDLIKVKDE KIRQAFYFAL RDTLVADNLD
     QATRVAYQKD RRWRVVTLQG QIIEQSGTMT GGGTRVAKGR MGSSVVVEIS EEQVNKMELQ
     LQKDSQKAAQ IQEQKVRLEE AVLKLRHSER EMRNTLEKFT ASIQRLSEQE EYLNVQVKEL
     EANVLATAPD KKKQKLLEEN VTTFKTEYDN VAERANKVED EVKRLHSLII EINNHKLKAQ
     QDKLDKINKQ LDECASAITK AQVAIKTADR NLKKAQDSVF RTEKEIKDTE KEVEDLTAEL
     KNLEEKATEV IQNTNAAEES LPEIQKEHRN LLQELKVIQE NEHALQKDAL SIKLKLEQID
     GHITEHNSKI KYWQKEISKI SLHPIEDNPV REISILSPED LEAIKNPDSI TNQIALLEAQ
     CHEMKPNLGA IAEYKKKEEL YLQRVAELDK ITSERDNFRQ AYEDLRKQRL NEFMAGFYII
     TNKLKENYQM LTLGGDAELE LVDSLDPFSE GIMFSVRPPK KSWKKIFNLS GGEKTLSSLA
     LVFALHHYKP TPLYFMDEID AALDFKNVSI VAFYIYEQTK NAQFIIISLR NNMFEISDRL
     IGIYKTYNIT KSVAVNPKEI ASKEL
//