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Database: UniProt
Entry: A0A0V0UYU0_9BILA
LinkDB: A0A0V0UYU0_9BILA
Original site: A0A0V0UYU0_9BILA 
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}.
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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
//
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