ID   A0A3B3XMB4_9TELE        Unreviewed;      1248 AA.
AC   A0A3B3XMB4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000016162.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000016162.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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. SMC2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005231}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B3XMB4; -.
DR   STRING; 48701.ENSPMEP00000016162; -.
DR   Ensembl; ENSPMET00000024652.1; ENSPMEP00000016162.1; ENSPMEG00000018825.1.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   CDD; cd03273; ABC_SMC2_euk; 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; 4.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR027120; Smc2_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 2.
DR   PIRSF; PIRSF005719; SMC; 3.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
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   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          580..700
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          280..328
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          355..399
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          443..505
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          535..562
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          734..990
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1044..1092
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1248 AA;  141361 MW;  EECC0FD58E06BB26 CRC64;
     MYIKSIIIEG FKSYAQRTEI NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLTHVRAS
     NLQDLVYKNG QGGITKATVS ITFDNSNKSQ SPLGFETHDE ITVTRQVVIG GRNKYLINGV
     NANNTRVQDL FCSVGLNVNN PHFLIMQVGC FITFLPFFFF FVFKTSNIRL SFDLVMFLSL
     QGRITKVLNM KPPEILAMIE EAAGTRMYEC KKISAQKTIE KKEAKLKEIQ TILDEEITPT
     MQKLQEERSS YLEYQKLMRE IQHLSRLYVA WLFMCAEETK KKSAENLKVM QDNIAKMQAN
     MAENESKIQE LSAQIQEQQK KRDQEVNGVL KTLEDTLADA QRVDAKSQSA LDLKKQNLKD
     ETKKRKELVK SMEEDKKMLV VKEKEVSKLA EQLRAVQEEG QKDSAALEAA EQHFKAVSAG
     LSTNEDGEED TLAGQMMACK NDMSKADTEA KQAQMTLKHA QAELKSKQAE VKKMDSGYKK
     DQDALQAARS SREKLEAGLA KLNYEGSKRL LPSFSFISPL NQCDNCGCVS AEGKEESLLE
     NRRQLSRQVS QLKETYERLM SRFPNLRFDY KDPERGWDRS KVKGLLANLI TVSDVTYATA
     LEVVAGGRLY NIVVDTEVTG KKILEKGELQ RRYTIIPLNK ISAKTLNDKV INAAKSLVGQ
     DNVHTSLSLV GYEADLRKAM EYVFGSTLVC DTLDNAKKVA FDKQVMTKTV TLGGDIFDPQ
     GTLSGGARSQ SASILTSLQE VKEVQDRLEE KEAQLQDVER QLADLKGTAE KYRQLKQQHE
     LKLEEEQILQ AKVQQSSFHQ QQEELERLRK AIEESEETLR VTKEVKKKAE EKYKVLENKM
     KNAEAEREKE LKAAQEKLNT AKAKADAFNK KLKQKQQESD AVALELEELQ REQAGYEQQI
     QAVDEATKAI QEQIDSMACT VSQNKETVRK AQEELSKQKE VIMTQDKELK EKNTEVNKMR
     EKNNEAQLKI KELEHNINKH HKESQDAADK VSRMLEEHDW IHSERQYFGQ PNTSYNFKTN
     NPREAGQRLK KLEETTSKLE RNVNKRAMNM LNEAEERYND LMKKKRIVEN DKAKILQTIK
     ELDQKKNEAL NLAWQKVNKD FGSIFSTLLP GATAKLAPPQ GCGVLDGLEF KVALGDTWKE
     NLTELSGGQR FETLCCSLVC FLSLCENVTL ISLSLSLYLS LSLSLSLLIR SLVALSLILA
     MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQV SDSKKAIY
//