ID A0A0V0ZSL4_9BILA Unreviewed; 1199 AA.
AC A0A0V0ZSL4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Amyloid beta A4 protein-binding family B member 2 {ECO:0000313|EMBL:KRY15453.1};
GN Name=CCNH {ECO:0000313|EMBL:KRY15453.1};
GN ORFNames=T12_15847 {ECO:0000313|EMBL:KRY15453.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY15453.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY15453.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY15453.1};
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 -!- SIMILARITY: Belongs to the IPP transferase family.
CC {ECO:0000256|RuleBase:RU003785}.
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:KRY15453.1}.
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DR EMBL; JYDQ01000095; KRY15453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZSL4; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd01272; PTB1_Fe65; 1.
DR CDD; cd01271; PTB2_Fe65; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.20.140; -; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039576; APBB1/2/3.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR NCBIfam; TIGR00174; miaA; 1.
DR PANTHER; PTHR14058; AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING FAMILY B; 1.
DR PANTHER; PTHR14058:SF8; PROTEIN FE65 HOMOLOG; 1.
DR Pfam; PF01715; IPPT; 1.
DR Pfam; PF00640; PID; 2.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01179; PID; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003785};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003785};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003785}.
FT DOMAIN 723..756
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 863..999
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 1035..1156
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 640..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 136913 MW; 736C2EFB8799C17C CRC64;
MLWLIRNYET LLNYEMISCY TGNMRCGVDW KKPIVVILGA TGTGKTELAV EVCLHAGGEM
ISADAMQMYS GLAIATNKST VEERRNVDEH LVSSLHPLTF GYSVQHFRQQ ALQTIAAVQS
RGRLPVLVGG TNYYIESLIW NTLLSENQPP HTGNCYYQDL PADLLTMDGE RLLDELRKVD
PDMACRLHPN NRRRLLRSLQ VWHATGRRQS ELVEQQRLSD VEQKLLFQNC LILWLRIDRQ
LLHKRLEARL KRMLERGLKD ELVEFYDTFY DQYVAKQNSI PDDNQAKGAF QCLGFKEFLP
FLRLEPEARH STHGLEIFQR CLEQLHLATC RYAKKQVKWI ENRIVRRPGS VALPVYALNM
HADTPHSFRH CIAQALTLVD WFLSPATVPP VMEPLNQKSL DWKAHDDKLL YVRCETCNRF
FDCRYSNSLK EEALAVFFLV QQCHICSGKS NSTPSFCWVE QVFLETQAKW TMATAAVAAS
TRCSDDGIFG KQTVSNANVR MEKIVTEIQH DNNNSCAEEG VDCYDGATSD LVETNRSERE
LVLNIGNSAT TTIEEPLSRL GMSAGDETMS SFRPSLDRRL EDSVDYGAND FQRSFDAINK
AALNSAGFRI RRHHDANVVT QHRDPYSFYW HSSTMDNANL GDDYNDNDND KGGSTNHLPA
RDNSVEEFYA TDDVAHVKSP DSHDSGIQME YAQPSKPVRR LPDYLIQPFE NEQENDNDES
PRRPLPPGWE QHEDPRGFSY YWHVDSGTVQ RERPTESMKK LNCSPWYYLL FAMLHAVSVW
KALAYSELTG LVKTLNYESQ SDTSESSEQS EQKTKHNRSA TPLEQPIIVE RAFKQTTLKR
RVERDSSSSE RNTCEEADSR GPVRFAVRSL GWTEIAEENL TPEKSSRAVN RAIVDLSTGR
NDFMDNVSKW GDGKELIMEL DDHDLRLCDP DSDTVLHVQP IHQIRVWGVG RDNGRDFAYV
ARDRNSRRFM CHVFRCDTPA RTIANTLRDI CKRLMMEKRP NSLLPGRNEN SHRRKPVVVD
SFPTPMEEPK KVIRAHFLGV TQVPKATGVD VLNEAVDRLV AQVRSERWIL VDVSIAPSTI
TVTEVGGNQI AECRVRYLSF LGIGRDIKHC AFIMHMSTEN YMCYVFHVEP SAGAMAKTIE
AACKLRYQKV IDAHGERRTA SKVRWATFPG WSESIRDIFG NLSGHRRSAN NPARQHYAA
//
