ID   A0A2K5ES66_AOTNA        Unreviewed;      2005 AA.
AC   A0A2K5ES66;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Structural maintenance of chromosomes flexible hinge domain containing 1 {ECO:0000313|Ensembl:ENSANAP00000036061.1};
GN   Name=SMCHD1 {ECO:0000313|Ensembl:ENSANAP00000036061.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000036061.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000036061.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 37293.ENSANAP00000036061; -.
DR   Ensembl; ENSANAT00000054132.1; ENSANAP00000036061.1; ENSANAG00000035458.1.
DR   GeneTree; ENSGT00390000006950; -.
DR   OMA; PRGEHIM; -.
DR   OrthoDB; 5388904at2759; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0001740; C:Barr body; IEA:Ensembl.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0060818; P:inactivation of paternal X chromosome by genomic imprinting; IEA:Ensembl.
DR   GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0043584; P:nose development; IEA:Ensembl.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   CDD; cd16937; HATPase_SMCHD1-like; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   InterPro; IPR038892; SMCHD1.
DR   PANTHER; PTHR22640:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES FLEXIBLE HINGE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR22640; UNCHARACTERIZED; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT   DOMAIN          1720..1847
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
SQ   SEQUENCE   2005 AA;  226253 MW;  47955952BCF06A08 CRC64;
     MAAADGGGPG GASVGTVEDG GGVGHRTVYL FDRREKESEL GDRPLQVGER LDYAGFRATV
     CQTLGISSEE KFVITTTSRK EITCDNFEET VKDGVTLYLL QSANQLLLTA TKERIDFLPH
     YDTLVKSGMY EYYASEGQNP LPFALAELID NSLSATSRNT GIRRIQIKLL FDETQGKPAV
     AVIDNGRGMT SKQLNNWAVY RLSKFTRQGD FESDHSGYVR PVPVPRSLNS DISYFGVGGK
     QAVFFVGQSA RMISKPADSQ DVHELVLSKE DFEKKEKNKE AIYSGYIRNR KPSDSVHITN
     DDERFLHHLI IEEKEKDSFT AVVITGVQPE HIQYLKNYFH LWTRQLAHIY HYYIHGPKGN
     EIRTSKEVGP FNNIDIEISM FEKGKAPKIV NLREIQDDMQ TLYINTAADS FEFKAHVEGD
     GVVEGIIRFH PFLYDRETYP DDPCFPSKLK DEDDDDDCFI LEKAARGKRP IFECFWNGRL
     IPYTSVEDFD WCTPPKKRGL APIECYNRIS GALFTNDKFQ VSTNKLTFMD LELKLKDKNT
     LFTRILNGQE QRMKIDREFA LWLKDCHEKY DKQIKFTLFK GTITRPDLPS KKQGPWATYA
     AIEWDGKIYK AGQLVKTIKT LPLFYGSIVR FFLYGDHDGE VYATGGEVQI AMEPQALYDE
     VKTVPIAKLD RTVAEKAVKK YVEDEMARLP DRLSVTWPEG DELLPNEIRP AGTPIGALRI
     EILNKKGEAM QKLPGTSHGG SKKLLVELKV ILHSSSGNKE IISHISQHGG KWPYWFKKME
     NIHKLGNYTL KLQVVLNESN ADTYAGRPLP SKAIKFSVKE GKPEKFSFGL LDPPFRVGVP
     FNIPLEFQDE FGHTSQLVTD IQPVLEASGL SLHYEEITKG PNCVIRGVTA KGPVNSCQGK
     NYNLKVILPG LKEDSQILKI RLLPGHPRRL KVKPDSEILV IENGTAFPFQ VEVLDESDNI
     TAQPKLIVHC KFSGAPNLPV YVVDCSSSGT SILTGSAIQV QNIKKDQTLK ARIEIPSCKD
     VAPVEKTIKL LPSSHVARLQ IFSVEGQKAI QIKHQDEVNW IAGDVMHNLI FQMYDEGERE
     INITSALAEK IKVNWTPEIN KEHLLQGLLP DVQVPTSVKD MRYCQVSFQD DHVSLESAFT
     VRPLPDEPKH LKCELKGGKT VQMGQELQGE VVIIITDQYG NQIQAFSPSS LSALSVAGVG
     LDNSNLKTTF QENTQSISVR GIRFIPGPPG NKDLCFTWRE FSDFIRVQLI SGPPAKLLLI
     DWPELKESIP VINGRDLQNP IIVQLCDQWD NPALVPHVKI SLTKASNLKL MPSNQQHKTD
     EKGRSNLGVF SVFAPRGEHT VQVKAIYNKS IIEGPVIKLM ILPDPEKPVR LNVKYDKDAS
     FLAGGLFTDF MISVISEDDS IIKNINPARI SMKMWKLSTS GNRPPANAET FSCNKIKDND
     KEDGCFYFRD KVIPNKVGTY CIQFGFMMDK TNILNSEQII VDVLPNQPVK LVPKIKPPTP
     AVSNVRSVAS RTLVRDLHLS ITDDYNNHTG IDLVGTIVAT IKGSNEEDTD TPLFIGKVRT
     LEFPFVNGSA EIMSLVLAES SPGRDSTEYF IIFEPQLPLL SKTLEPYILP FMFYNDVKKQ
     QQMAALTKEK DQLSQSIIMY KSLFEAGQQL LNEMKCQFED ARLKEAQLRN ELKIHNIDIP
     TTQQVPHIET LLKRKLSEQE ELKKKPRRSC TLPNYTKGSG DVLGKIAHLA QIEDDRAAMV
     ISWHLASDMD CVVTLTTDAA RRIYDETQGR QQVLPLDSIY KKTLPDWKRP LPHFRNGKLY
     FKPIGDPVFA RDLLTFPDNI EHCETVFGML LGDTIILDNL DAANHYRKEV VKITHCPTLL
     TRDGDRIRSN GKFGGLQNKA PPMDKLRGMV FGAPVPKQCL ILGEQIDLLQ QYRSTVCKLD
     SVNKDLNSQL EYLRTPDMKK KKQELDEHEK NLKLIEEKLG MTPIRKCNDS LRQSPKVEMT
     DSPIPPKRMR REVTRQNRII TKTDV
//