ID A0A0V1HMH2_9BILA Unreviewed; 3651 AA.
AC A0A0V1HMH2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Protein unc-45 homolog B {ECO:0000256|ARBA:ARBA00020768};
GN Name=Ubr5 {ECO:0000313|EMBL:KRZ11718.1};
GN ORFNames=T11_18159 {ECO:0000313|EMBL:KRZ11718.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ11718.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ11718.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ11718.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band
CC {ECO:0000256|ARBA:ARBA00004161}. Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000256|ARBA:ARBA00004216}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}.
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:KRZ11718.1}.
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DR EMBL; JYDP01000047; KRZ11718.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR CDD; cd14423; CUE_UBR5; 1.
DR CDD; cd19675; UBR-box_UBR5; 1.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR047503; UBR-box_UBR5.
DR InterPro; IPR024725; UBR5_UBA.
DR InterPro; IPR024660; UCS_central_dom.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR46276; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR PANTHER; PTHR46276:SF1; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR Pfam; PF11547; E3_UbLigase_EDD; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF11701; UNC45-central; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00028; TPR; 3.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REPEAT 5..38
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 78..111
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 2035..2103
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 3129..3206
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT DOMAIN 3328..3639
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ZN_FING 2035..2103
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1055..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2401..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2464..2543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2644..2675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2877..2905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3080..3107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2464..2484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2485..2507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2653..2675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3606
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3651 AA; 404141 MW; 83A7860606AD8893 CRC64;
MAEEVNNLKA EGNLYYEAGN WEKAKEYYNK ALKACPSEDK ITLAALLKNM AAVSLKLEDY
VAAENQASQA LECAPNDPKA LYRRSTARSY LSKYSEALTD VKRALHYEPD NKAIIKQFQD
LNIMIQKNAE KLGSTEAKLQ DMLKICFSVE ATLENRIQAL HNIMVLVGYD DGARLFTECG
GLARLMKLID DESDTDLLLA AFRVLIELAT SEERLGFLFK VADSKTIVYL LNCSDNRCCQ
AAMALVQRCF NTLSAMDFQK QKLPDEIVVE RNKVKIVGFL FELKRILVDP TVSAMGRDCA
IQLLSKILPH RVGGLPKGWS LEFVQNDGLD RLMTVGCSIP ERALVPVTYE TRDYLALCLT
NIYDDMLSDK NRNMYTDRME KFIQEKREKI TDGVKIEICS LFTTLLGGPV DVAFQFVAKP
EFTQLLLEMA ASDDQLNQSV AVEAIMHTVS KRDRCSVFLA QGKSVLKKLF NSSNDVVRVK
ALVGLCKISS SGGNDISMRP TGELSMLRLA NICKRYLLEN KSIDICRWAA EGLAYLTLDA
DVKEWLVSDV NLIRRLVAFA KQAGQLCVFG VSTILVNLTN TYDKKEPEPE LIELAKFAKH
HIPVANPKDS DEYVQNRIKL LVNEGAVSAC VALSSTESER CREFLARALH GFTKEPQHRG
IVVQEGGVKL LIDLAQRCTE EGKIIAAHAL ARIGITMDPK MAFSGQRCYE VVKPIISLLH
PDMSAEQNYE ALLALTNLAA VSDSVRNKMI QENVLPKLEE FWFLQEHEPL RAASAELFHN
LLLNDKIFEQ VAKPGTDRLK LWLLYCSADD DERLALISTS AVLLLTQDAA VCSRIVQEHP
NWPDLFKVPC MHENEQLQLN AIGCVKNLMN SGQEAAAQVV SSELFEILVA ICKLPKSNRE
KAVSLAYETL KLAVAYDLVK PTSRELYEQL TGKPTMVEHR TPTVMFRLNE EAVVVITFLK
YVDLSLECPL LKREAMNSFH RFAFSLPDKD LRLEQQLRDS MNSQALDAQS TFMFDMSPFR
PEDMKDIVVG PDAIAFLTVD GQVFRVAYDI IDDTRDHVNK GNDNGKKDAT GSGGGATGCS
TVQASNTGRG SGGPNNNNAG SGGNNDSNAG ISARATKIRR VMMARSRVGR GGVIVGSRPI
IPAGAVPEEL VNEAQAVLQG KSRDVIIREL QRTNCDVNQA VNNLLGRDDE DGDDFDDTSE
AYLPEELISL LDTGLQGEQA NVIINAESLY GDDFLSFPFR RRVFEKAAEK KTNDSASKES
SNEESVPPPP RYTISLSPKK MFFKWTTNEE SAAETKRFRA IGAMHSDLLA VSMDGVLYRW
AWNQKQPSPN PHPAWETICN KEPVESISCS SIRTTVLTTH RRVASFVDES LDLISNALST
SLHSLPEPIV DVYSCDLYSC AMTKSGNVYW WGVLPSVQRM KVLDAIKNKL KKEVASDAKD
ITVGRLVRMQ HGPMFQADAL GFTVVNGYPQ VVILMESVWP NHDTARFQML LPSSSVLDPK
RGLYNEGLES AVEDSSETFV SSAQLSAGNR KRKHALSAVS SYREETLHLK DVVMVVENRN
ATIGKVVKVD GPYCAVLFAD SNGVINDTAD DAMNRSRLLR KEDLRVVPKV QCFSSTLEYI
QREPKKFYNL SDDHFVLDVA IESTGIWYLH QLLGRVLLSK INFSGEMLAS IIVAYDSHEF
IGSRRPRLIN NGEDSLILIR DGCGSLTPVW TDLPARVGSP TGIGTVMALG YGTHTIASNF
SEKKKIGIIL LAEKKEELMR DILHCDVDYI KARLFSQKPM VTSRLYEDML SLKLNCGRNV
LHVAVSMSIA PTNKENFSLS LASQIAASEN PAGSRPPSDG RWEAVNSPSR INVTVSLNSM
MQLGRRFVDP TGMSSHVLRG YALRSDASTQ SAASRWAMEM AVEAAAAAAG IVPAGGSSST
TAVTAQSSSS SSSTPTMAVD EEMMVPASLD LSTLKPKALT SSIERQRAAD HNGMTPFMYA
IDCRSYHVAE IILLSLKRII RSFSAQNQNR AMMSVVFPVN TRPEFSPLYM LCCNDTCSFT
WTGSEHVNQD IFECITCGLV GSLCCCTECA YVCHRNHECR LKRTSPTAYC DCWEKCKCRS
LVAGNLDIRF ELFKSLISCQ SLYSVLNDKN EHLLLFLTRT VSRQVSEHRQ FRSRCRKSIA
SLIDMPEFDL DPPRFALRAL EYLFSRWDLF EHFVMHEYHP VETNINMSES RFYLISQDGV
SFLDRFVYLL LTKLPIGCFD SLVRLLSTEC KATSKVDKNL AVLPRFARSV VRMFVLLNVS
PQYSNCRKNQ PLSRCRKVFH AILPHAVREL VTTADGILAP VRLGMVKPCE PFTMANCTDP
LELIEKMVME DPVLLPNDVD KEEEKKFGVD ENDILSSSPI VVNSLPKRTR SEEVSYMQDL
ATLTGEEATS DNDTDSEVDE AMQEAEGNAT AGSDAGNDDS SVDVAMSPLE AMPTLHVVEI
PTEADSDHDG SQASGRHARR VSNADQDTDY SYTEVESNSS VSEESDVMFD ENNQEDTDTE
GSNFAWSGRV RDRKKGTKQT ASPEKLSTST VHITNLLSRL FSTLIREALD LLLYGYSSEQ
SSIASRSSST FYVPKRLLAE LLEQVSRTLQ PTWNWLFPLL DYLDSHLRFS AAMSNMVGPK
KRQAAKSHMS DIAGEGDSTQ TTADKSPIET SSKSETASRL TVLNLLMSVM RSHSSEHGDS
WAVLDLWSMK HVAIVADAYF CYAGALSMFS ENLCNSVRDM SKDFPASSCC DLLFIRALQR
DSSDPIAGES TSISKQNPFF TRSDSMVYPG LFPVRSAFEH SVPESIPLCN RPHMLQASSS
KESLYGLPAS SDKWSEHLRS QLQMGNEAPG SSSLTRSMSH KTRLILASFA PVDDSAADRE
IQKSSPKRFR RERRSKSVIV HSSEAASPKS AEDTIAAIVN SALVRCEDQQ MLMSRWKLVL
STFAKIFTDE HVLTSGGSIF TQLAGFGPKA ARFRKAMERI RNTSKDLQFM VDRDRPLLLR
ETFQVLNAFF ERRQMGNSSQ HHAIGVHRVK VSFKDEPGEG SGVARSFFTA IASALLAPLP
LPNFELSPLP TTVLGMNTIG SPSAATPIPP TRQRLGLRSR GRSKDNSRRP LFTMPVGWLE
GTIGASPFFP TVSAPEVAGP LDENNVQAMG NRIYMKVNSM FPRYAAKVTG MLLEVPTHQL
IVMLTHEATL EHLAQNAYEV LLTWVQSSGN LGDFMPGGPL TSASTTSTLM PSTVATAQPA
NNATVTTTIA TASTASASVS ASQVSSVAVS GAAAATTSMA AVDASSSAAS SGGGSTSTVS
PPAAGAAIQS TVSTYDSRWL SCPDLPRLLE NVADVKDDRP LFFKPGNGMF YAPVAGAESP
SRLNAYRNVG RLIGIALSQN EIFPLPLCRS VFKFILRRPI TWYDMAFYDC YMYEKLHKLV
TGEYAAEDLD LNFTITLDAI EGGNTVELLS DGANVTVTSE NVVKYVFLYA QHRLYKLVQS
ALTSIRDGVR DVIPVSVLDT INAEDFRLLL TGQSDVNVKF LKKLTVITDE SSSAAADKSL
PREKFDQFKK WFWSVVSCMT ADEKQDLIYF WTGSPTLPPT MEGFMPTPNV VIRPPDDMYL
PTANTCISRL YIPLYSSKNI LRQKLLFAIK IKTFGFNTVI KKNTGSEEEK I
//
