ID A0A0V0ZS72_9BILA Unreviewed; 1475 AA.
AC A0A0V0ZS72;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Amyloid beta A4 protein-binding family B member 2 {ECO:0000313|EMBL:KRY15451.1};
GN Name=CCNH {ECO:0000313|EMBL:KRY15451.1};
GN ORFNames=T12_15847 {ECO:0000313|EMBL:KRY15451.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY15451.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY15451.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY15451.1};
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 -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000256|ARBA:ARBA00008638}.
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:KRY15451.1}.
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DR EMBL; JYDQ01000095; KRY15451.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V0ZS72; -.
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; cd20524; CYCLIN_CCNH_rpt1; 1.
DR CDD; cd20525; CYCLIN_CCNH_rpt2; 1.
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; 1.10.472.10; Cyclin-like; 2.
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; IPR036915; Cyclin-like_sf.
DR InterPro; IPR031658; Cyclin_C_2.
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; PF16899; Cyclin_C_2; 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; SSF47954; Cyclin-like; 2.
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 1006..1039
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1146..1282
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 1318..1439
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 923..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 168899 MW; 333C1265E6DA82F3 CRC64;
MFSNSSQKRY WMFDSMQTLT SIRHQSRQRF HEKMQERAGV EFDSSVLLTE EEERLVCSVV
EENALKFCQN FSPPLPWSTI CTAFCLFKRF YLQTSVSEFV VAKNVMMAII YLACKLDDFY
VTIETFTQKL KSGTQAENAE VILSLEMEVL TRIKCHLYVY HPFRPLEGHF ISMKTLYPEF
EKVELLRQGA YDFLWNSLFT DVSFLYSPSQ IALAALLASA KQNMAEIAVE QYIRNAMRSC
ELKQINALLL KVKECCDMVA SREPVPPSYH ASIQLRIKQC AEYVNKFFPQ GDEVYIKVIK
QNYKRNMRCG VDWKKPIVVI LGATGTGKTE LAVEVCLHAG GEMISADAMQ MYSGLAIATN
KSTVEERRNV DEHLVSSLHP LTFGYSVQHF RQQALQTIAA VQSRGRLPVL VGGTNYYIES
LIWNTLLSEN QPPHTGNCYY QDLPADLLTM DGERLLDELR KVDPDMACRL HPNNRRRLLR
SLQVWHATGR RQSELVEQQR LSDVEQKLLF QNCLILWLRI DRQLLHKRLE ARLKRMLERG
LKDELVEFYD TFYDQYVAKQ NSIPDDNQAK GAFQCLGFKE FLPFLRLEPE ARHSTHGLEI
FQRCLEQLHL ATCRYAKKQV KWIENRIVRR PGSVALPVYA LNMHADTPHS FRHCIAQALT
LVDWFLSPAT VPPVMEPLNQ KSLDWKAHDD KLLYVRCETC NRFFDCRYSN SLKEEALAVF
FLVQQCHICS GKSNSTPSFC WVEQVFLETQ AKWTMATAAV AASTRCSDDG IFGKQTVSNA
NVRMEKIVTE IQHDNNNSCA EEGVDCYDGA TSDLVETNRS ERELVLNIGN SATTTIEEPL
SRLGMSAGDE TMSSFRPSLD RRLEDSVDYG ANDFQRSFDA INKAALNSAG FRIRRHHDAN
VVTQHRDPYS FYWHSSTMDN ANLGDDYNDN DNDKGGSTNH LPARDNSVEE FYATDDVAHV
KSPDSHDSGI QMEYAQPSKP VRRLPDYLIQ PFENEQENDN DESPRRPLPP GWEQHEDPRG
FSYYWHVDSG TVQRERPTES MKKLNCSPWY YLLFAMLHAV SVWKALAYSE LTGLVKTLNY
ESQSDTSESS EQSEQKTKHN RSATPLEQPI IVERAFKQTT LKRRVERDSS SSERNTCEEA
DSRGPVRFAV RSLGWTEIAE ENLTPEKSSR AVNRAIVDLS TGRNDFMDNV SKWGDGKELI
MELDDHDLRL CDPDSDTVLH VQPIHQIRVW GVGRDNGRDF AYVARDRNSR RFMCHVFRCD
TPARTIANTL RDICKRLMME KRPNSLLPGR NENSHRRKPV VVDSFPTPME EPKKVIRAHF
LGVTQVPKAT GVDVLNEAVD RLVAQVRSER WILVDVSIAP STITVTEVGG NQIAECRVRY
LSFLGIGRDI KHCAFIMHMS TENYMCYVFH VEPSAGAMAK TIEAACKLRY QKVIDAHGER
RTASKGWSES IRDIFGNLSG HRRSANNPAR QHYAA
//
