ID A0A176VDV7_MARPO Unreviewed; 1147 AA.
AC A0A176VDV7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN ORFNames=AXG93_1923s1280 {ECO:0000313|EMBL:OAE18572.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE18572.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE18572.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE18572.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005231}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE18572.1}.
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DR EMBL; LVLJ01004028; OAE18572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VDV7; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000077202; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; 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; 2.
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; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 518..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 239..280
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 324..379
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 407..493
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 788..927
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 966..1029
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1147 AA; 129608 MW; D4ABA7B14DE9720F CRC64;
MYVKEVTLEG FKSYAQRTVV SGFDPFFNAI TGLNGSGKSN ILDSICFVLG ITNLQQVRAT
NLQELVYKQG QAGITKATVS ILFDNSDRNR SPIGYEDMNE ITVSRQIVVG GRNKYMINGH
VRQPAQVQNL FHSVQLNVNN PHFLIMQGRI TKVLNMKPPE ILSMLEEAAG TKMYESKKEV
ALKTLEKKQT KVDDIDNLLK QDILPALEKL RKERAQYQQW TSGNAQLDRL ERFCTAFEYS
EAERIKNAAS DVVKDMESQI KALQVTAVEL EKEIGDKESS IASMTETKDK EMSSEIKILS
DVSDKLSTTL VTLDSALNAK RDACKAEKAA LEQIQRSKKE LENAIAARTT SEKQIEEDVA
ALQEKVDKSR KHLEDIESEY QAVQAGKGSG ADDMSLAEQL ADANVSVGKS ASELQQLQTK
IQHLNKELME KREYFKSKEH EVAAAQEELK SRKADLANLK SAIDKIGYRD GSMQVLEEKR
RQEVEYVKKL KADVNNLTSQ LSGVQFSYSD PERDFQRSRV KGVVARLVHV NDSSAMTALE
VIAAGKLFFV IVDNDQTAKL LLEKGNLRRR STIIPMNKIQ PNKIPARVEA VATKLVGSKA
KPALSLVRYA DELEAAMSFV FGGTFVCADT ETAKQIAFHK EIMTKSVTFP GDVFEPRGLL
TGGSRKNGGE LLVQLHALAE TEARLIHHED ELKNVELKIE SLLPQQKKFS HLKSQMELKS
YDLSLYETRA QQSEHHKLSE VIALMTSELD KEKSALTRTQ QYHSECQKRV FQIEQKIKDQ
GRDRDSLLKD LEKRIKSMKK EAVAATKELK EQEGAKERMV MEKEAAVQEI LTLEDQLATA
HTQITKLETD LREKETKRGA IEEEYQKAKG KLEENRKRIK ECDAQITALV KSQNQQKNKL
TDCIVEIKKL ENEIKRLGMN QKECDKRVQQ LLAKHEWIVR ERQAFGKAGT DYDFTAQDPR
EARQALESLQ REQKDIEKRI NKKALAMFDK AEEEYNDLIE RKRIVQNDKT KIQQVIKELD
EKRKEQLKNT WEKVTKEFGS IFSTLLPGTM AKLEPPEGAD VMDGLEVKVA FGSVWKQSLS
ELSGGQRSLL ALSLILALLL FKPAPLYILD EVSAKFEFAS QNFLDDFSYV EAIAGIGDCL
MECFLAG
//
