ID A0A421JU63_9ASCO Unreviewed; 1730 AA.
AC A0A421JU63;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Structural maintenance of chromosomes protein 1 {ECO:0000313|EMBL:RLV95469.1};
GN ORFNames=JA1_001098 {ECO:0000313|EMBL:RLV95469.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV95469.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV95469.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV95469.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
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:RLV95469.1}.
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DR EMBL; NSGQ01000005; RLV95469.1; -; Genomic_DNA.
DR STRING; 2028339.A0A421JU63; -.
DR Proteomes; UP000285775; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; 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:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:InterPro.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:UniProt.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 2.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR025795; tRNA_(uracil-5-)_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR18937:SF12; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS51622; SAM_MT_RNA_M5U_2; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT DOMAIN 532..647
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 257..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 341..368
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 403..444
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 691..718
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 760..794
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 834..938
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1028..1055
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 1683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 1683
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1555
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1584
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1606
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1656
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 1730 AA; 198167 MW; BCF16F8629954BDF CRC64;
MGRLIGLELF NFKSYKGKTT IGFGSSFFTS IIGPNGAGKS NMMDAISFVL GIKSSQLRSA
NLSDLIYRAR KVTGGTTAAD ALDADDTTLN SVEPDPTSAY VMAIYEKDDG EILKLKRNIT
LNGSSDYRIN NRSVTLLNYT KVLKQENILI KARNFLVFQG DIEQLASKSA KELTGTLEQI
SGSDEYVQEF DQLKEEVERA KEVSISVFSK KRTLNSESKQ YKEQMAEQIE FEEKLVIKSD
TIKKIHLYKL YHNERKHQLL HQEIKQKKHD LKQCKQDLKT KEKLYESMMS EYSGIVLDSN
KMKSKVTANE NKLESIHRDL IPIEANKRAL ASKIASRRNK IVDLTKDIEN QKVQVVNISN
QLRDAERLSR EFDQQNKSDN IAISPEAQQE YSSLRSKFLT TEESRLEQDL TLLTNEQDQL
KANIRNVESQ RDHAETTVRD LQSQLSTDLK SKFDDITTEI NNILEFKTDK DDLRKSLIKI
KNDYESKHGQ LSIQYRDALT KINDSNSQQQ ESSKQRQLRE NVAMLQQSFP QGDIRGLVYE
LVRPTMSKYE NALATLLGRN FDAIIVKSSS IAHKAIEILK ERRAGVATFI PLDTIDVETI
NLHHLRSVAV PGVDIMEYDD KSLENAMNYI AGDALIVENM NVARELKWQT GKVNNKLITL
QGNVIHKSGF MTGGGSSQKP TAVVNWDKRE YVRLTQAKDE LEVQLRKLEE EMPKSIEISL
LAEEISQFDD KLVMLRDDKD NIDRVIKDRE SEIEFENKLA KEFSNTIEQK LNEVNHLQGR
INELSNKIRS AKHEIFHEFC DRYGFVNGIE DYEKTHGNTL RTKARERIQY SKAISTLTNK
LEFEQGRLNK TEERKVSLES QIVELQGEFD QVLLEKNRLQ ESLDSIEAET EILKQELVNI
NNSVATKLKV TKSVESDVHE AESELNSINK QLFQIEEKLL KIDSERALEL INCRIQNINL
PLLEGDLENI PVGEDTTQQE ISEKIYEIEL DYSLLEAKFQ ESYNIHLESE LKAKLTTILE
ELEQVTPNIK AKDRLKDVEA KLREQDRDFS VARQQERITQ KKFQEVKEKR HEKFMDAFNH
ISSQIDIIYK ELTRSSVAPM GGSAYLTLED SEMPYLAGIK YHAMPPMKRF QDIENLSGGE
KSMAALALLF AIHSYQPSPF FVLDEIDASL DYANVVKIGN YIRNNCGPNF QFIVISLKNS
LFERSDALVG IYREQRENSS KTVTLDLKEY PEEEVVIANY NARPYTEREA NQYLKGIKQI
QGTKRRKDVQ DQTHPRRILH REINDFIKAR GVSSDQTANS DYFILYSFFE MKGHNVKVKA
SILGMTSSGL GIALVPKHEY APDFPTGDGK SFTVVLVPKT YTGDEVTIII KKHYEMYAEG
EYITIDNENT HRNNSLVKCK HFHECSGCQF QMVPYEEQLN FKQTTIQHAY QYFHPKLSQS
KSFGRVFGSP LQYEYRTKLT PHSRSFQGSI ITGFQSITSN HVIDIEQCSI ASPEIQDAYP
KYKQRLKQEN SKTSMIIRNS VDPTGNQIAL EGWKQIITEQ VENYKYQFDS SSFFQTNNVI
LPLVLDYIRS HIPPNSIDNL IDTYCGVGFF GIALNQTVQD KVVGIELSQK MIQYANHNVT
LNKLDSTRIK FIEGDASNIF SSISGMKGQR NMVIVDPSRT GSNKQFLTQL LDFAPDLIVY
ISCNVFTQAR DLAMFDELSN DVKYKVQDIV GFDFFPQTKH VETVAILEKV
//
