ID A0A0V0UYU0_9BILA Unreviewed; 1814 AA.
AC A0A0V0UYU0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Structural maintenance of chromosomes protein 1A {ECO:0000313|EMBL:KRX56462.1};
GN ORFNames=T09_12629 {ECO:0000313|EMBL:KRX56462.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56462.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX56462.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX56462.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680}.
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:KRX56462.1}.
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 EMBL; JYDN01000122; KRX56462.1; -; Genomic_DNA.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; 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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 1.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF12; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 511..630
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT DOMAIN 1687..1814
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT COILED 161..219
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 263..290
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 319..360
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 412..488
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 811..931
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1814 AA; 208817 MW; 9867B34688DE2B4B CRC64;
MGFLREIELE NFKSYKGYQR IGPFKKFTAI IGPNGSGKSN LMDAICFVLG EKTSSLRVRK
ISDLIYGAPV GKPVSTRCYV AMTYEDDDGR ILKFMRLVAG ASAEYRIDGA TVSHLQYTEA
LESINIFIRA KNFLVFQGAV ENIAMKNPKE CTLLFEEISR SGELKAEYET LKAEMMRAEQ
DTQLNYHRKR DIAAKRRAAK MEKEEAEKYQ KLKDSVAEKQ SRYYLMKLFS NDRESKRIFG
EMNGKHGEQS RIATKCSEVE EVLKERRKVY SKVTREVNKL EQQIYEMESE ITREKPSFIK
VKENVRHSER KLESFHKAFE AARKNAERQQ EVIRQFEVQL KEANEQRDAF EAQLMQESES
QGLQLDSEQL AQYNSLKGEV VRQCASIQQE LDVLAREQQM DQELLDNDKR CNGEFCQKIK
QKESELEALK KRLEKLVDTI RNTENEIEEQ RSSLRSTEDE VRTAKTRLEQ VIVEVEDVNR
QLNDANVDSS ENSRIVKKQE LVENLKRIST GTVYGRVVDL CQPAHKRYQL AVTKILGKYM
NAIVVDTEKT AKECIQYMKE QRIESETFLP VDYIDVKPLN EKLRELREPR NVKLIFDVIQ
FEPPQIRRVV QFACGNSLVC ESVEDARNLA FSGAERHRAV ALDGTVFEKS GIISGGAGDL
KAKAKRWDEK AVAHLRSRKS ALIEEQKELH RIRRKEPDIS LMQNSVKQLE TRMKYMLTDK
ENTKFETAMM ISQETRLLKN LESDLMQLKA ETEKYGPRIQ EIENRMASRR SNILQNQSRM
NQVADHVFAD FCKSIGVLNI RQYEEREIRF RQDKKQKMME FDNQIEKLKN ELEYQKSDDK
SGTVISAGIA ELAQLEKIEA SCNKEERELI KAKKEEQEHI RLLADLESQL KDLKAMRQTK
KVELENKEAE LNEVKKELAT IQKELLSVQK QTSAMETLLE QKRSERHSLL QTCKLENITL
PIIRGSLDIL GTTVSSQSSD TTSSVVSEDG ATTLSSTSFM GNRQLYQLEA EITFDFSSLN
PDDWELSDDT ELRLAAEKLL KEIGETQAFL QTITAPNLKA SAKLEGVRER FAETSGEFEQ
ARKKAKNAKM AFEIIQKERC SRFNRCFDQV SGKIDEIYKA LSRNFSSQAY LTADNPEEPY
LDGVSFSVVA PGKRFRPMDS LSGGEKTLAA LTLLFAIHSY NRAPFFVLDE IDAALDNTNI
GKVAAFIREQ AANNMQLIVI SLKEEFYNQA DALIGIYSVV CVYMTGSSIA SSGLLTLDLT
DYSETILNEE MINSLLFLSL RNAPVSYSKD WHNYTQMMLD RARRGVGEHG NPVELPSSVA
EKAEFDRLYK ANGYSGWTSD KISLYRAIKD LRHADCKRKS YLLLLPSTSV IVPFHNEHLS
VLLRTVYTIV YRTPPELLLE VILVNDASTK PELNDILERH VQRKFPNLVH VIRAGSDGRR
EGLIRARLRG KNVACMCCWA AKASGQVLMF MDAHSEVGYN WLPPLLEPIK LHYRTVTCPF
IDVIDCDTFA FRAQDEGARG SFDWKFHYKR LPLLNKTGAE PFESPVMAGG YFAISKRWFD
ELGRYDDQLM IWGAEQYELS FKLWQCHGRM IDIPCSRIAH VYRCKYAPFE DPGIGNFLER
NYKRVAETWM DEYKEYLYLR MPRLRNVDPG DLTKQREVRR RLKCNGFDWF MKNVMFDQPK
HYPLVEPPDV MSGRIKNKHT GRCMDVKNAG LQTELTTSQC KDYLKRQEFV LSWRSEIFQR
LGENCLDSMN HGPGETVHLF ACHGGGGNQN WTYSRNTTMH LQMTASNLCL DTDNTGRLFL
NTCQLVDSQK WLWS
//