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Conserved domains on  [gi|1519312720|ref|NP_004314|]
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BAG family molecular chaperone regulator 1 isoform BAG-1L [Homo sapiens]

Protein Classification

BAG family molecular chaperone regulator 5( domain architecture ID 10110639)

BAG (Bcl-2 associated athanogene) family molecular chaperone regulator 5 modulates proteostasis by inhibiting the activity of Hsp70 and several E3 ubiquitin ligases, resulting in enhanced neurodegeneration in models of Parkinson's disease

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
 144-221 2.70e-37

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


:

Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 128.55  E-value: 2.70e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519312720 144 LTVTVTHSNEKHDLHVTSQQGSsEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKK 221
Cdd:cd01812     1 LTVTVIHGSNKHTIELPSQDED-EPTLQDLAEAIEEVTGVPVENQKLIFKGKSLKDPEQPLSALGVKNGSKIMLIGKK 77
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
 246-326 3.92e-12

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


:

Pssm-ID: 214591  Cd Length: 79  Bit Score: 61.17  E-value: 3.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720  246 QLEELNKELTGIQqGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLIlPENFKDSRLKRKGLVKKVQAFLAECDTV 325
Cdd:smart00264   1 SIKKINEVLDEVQ-KKIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVD-VEGCEDIREARKRLVRLIQNLLNALDSK 78


                   .
gi 1519312720  326 E 326
Cdd:smart00264  79 K 79
PTZ00121 super family cl31754
MAEBL; Provisional
 64-138 1.36e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312720   64 AAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREE 138
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
 
Name Accession Description Interval E-value
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
 144-221 2.70e-37

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 128.55  E-value: 2.70e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519312720 144 LTVTVTHSNEKHDLHVTSQQGSsEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKK 221
Cdd:cd01812     1 LTVTVIHGSNKHTIELPSQDED-EPTLQDLAEAIEEVTGVPVENQKLIFKGKSLKDPEQPLSALGVKNGSKIMLIGKK 77
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
 246-326 3.92e-12

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


Pssm-ID: 214591  Cd Length: 79  Bit Score: 61.17  E-value: 3.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720  246 QLEELNKELTGIQqGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLIlPENFKDSRLKRKGLVKKVQAFLAECDTV 325
Cdd:smart00264   1 SIKKINEVLDEVQ-KKIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVD-VEGCEDIREARKRLVRLIQNLLNALDSK 78


                   .
gi 1519312720  326 E 326
Cdd:smart00264  79 K 79
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 156-220 1.35e-09

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 53.80  E-value: 1.35e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519312720  156 DLHVTSQQGSSEPV-------VQDLAQVVEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLIGK 220
Cdd:smart00213   2 ELTVKTLDGKTITLevkpsdtVSELKEKIAELTGIPPEQQRLIYKGKVLED-DRTLADYGIQDGSTIHLVLR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 157-221 2.65e-06

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 44.47  E-value: 2.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519312720 157 LHVTSQQGSSEPV-------VQDLAQVVEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLIGKK 221
Cdd:pfam00240   1 ITVKTLDGKKITLevdptdtVLELKEKIAEKEGVPPEQQRLIYSGKVLED-DQTLGEYGIEDGSTIHLVLRQ 71
PTZ00121 PTZ00121
MAEBL; Provisional
 64-138 1.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312720   64 AAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREE 138
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
 254-323 3.26e-03

BAG domain; Domain present in Hsp70 regulators.


Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 36.05  E-value: 3.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312720 254 LTGIQQGFLPKDLQAEALC------KLDRRVKATIEQFMKILEEIDTLILPENfKDSRLKRKGLVKKVQAFLAECD 323
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEgsppskKRDKEYKRLSEMLMKLLLKLDGIDTEGD-PEAREARKAAVKEVQGLLEKLD 75
 
Name Accession Description Interval E-value
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
 144-221 2.70e-37

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 128.55  E-value: 2.70e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519312720 144 LTVTVTHSNEKHDLHVTSQQGSsEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKK 221
Cdd:cd01812     1 LTVTVIHGSNKHTIELPSQDED-EPTLQDLAEAIEEVTGVPVENQKLIFKGKSLKDPEQPLSALGVKNGSKIMLIGKK 77
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
 246-326 3.92e-12

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


Pssm-ID: 214591  Cd Length: 79  Bit Score: 61.17  E-value: 3.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720  246 QLEELNKELTGIQqGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLIlPENFKDSRLKRKGLVKKVQAFLAECDTV 325
Cdd:smart00264   1 SIKKINEVLDEVQ-KKIEKEVQVADGKKDDKEYLRLSEELMKLLLKLDSVD-VEGCEDIREARKRLVRLIQNLLNALDSK 78


                   .
gi 1519312720  326 E 326
Cdd:smart00264  79 K 79
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 146-218 1.73e-10

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 56.07  E-value: 1.73e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519312720 146 VTVTH-SNEKHDLHVTSQQgssepVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLI 218
Cdd:cd17039     1 ITVKTlDGKTYTVEVDPDD-----TVADLKEKIEEKTGIPVEQQRLIYNGKELKD-DKTLSDYGIKDGSTIHLV 68
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 156-220 1.35e-09

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 53.80  E-value: 1.35e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519312720  156 DLHVTSQQGSSEPV-------VQDLAQVVEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLIGK 220
Cdd:smart00213   2 ELTVKTLDGKTITLevkpsdtVSELKEKIAELTGIPPEQQRLIYKGKVLED-DRTLADYGIQDGSTIHLVLR 72
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
 147-219 5.35e-08

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 49.17  E-value: 5.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519312720 147 TVTHSNEKHDLHVTSQQgssepVVQDLAQVVEEVIGVPQSFQKLIFKGkSLKEMETpLSALGIQDGCRVMLIG 219
Cdd:cd17047     4 KVIWNKEKYDVKFPLDS-----TIAELKEHIETLTGVPPAMQKLMYKG-LLKDDKT-LRELKVTKGAKVMVVG 69
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 144-218 2.01e-07

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 47.63  E-value: 2.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312720 144 LTVTVTHSN-EKHDLHVtsqqgSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETpLSALGIQDGCRVMLI 218
Cdd:cd16106     1 IKVTVKCSNgKKFTVEV-----EPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEET-LSSYKIQDGHTVHLV 70
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
 144-219 5.43e-07

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 46.46  E-value: 5.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312720 144 LTVTVTHSNEKHDLHVTsqqGSSEPVVQDLAQVvEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLIG 219
Cdd:cd16104     2 YKVNVKWGKEKFDDVEL---DTDEPPLVFKAQL-FALTGVPPERQKIMVKGGVLKD-DDDLSKLKLKDGQTLMLMG 72
Ubl_AtBAG1_like cd17054
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, ...
 146-218 2.17e-06

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, AtBAG2, AtBAG3, AtBAG4, and similar proteins; The family includes four Arabidopsis BAG family proteins (AtBAG1, AtBAG2, AtBAG3, AtBAG4) that have very similar domain organizations with a ubiquitin-like (Ubl) domain in the N-terminus and a BAG domain in the C-terminus. They may function as co-chaperones that regulate diverse cellular pathways, such as programmed cell death and stress responses. AtBAG1, AtBAG3, and AtBAG4 are predicted to localize in the cytoplasm, but the localization of AtBAG2 is the microbody. AtBAG4 can interact with Hsc70. The overexpression of AtBAG4 in tobacco plants confers tolerance to a wide range of abiotic stresses such as UV light, cold, oxidants, and salt treatments.


Pssm-ID: 340574  Cd Length: 70  Bit Score: 44.72  E-value: 2.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519312720 146 VTVTHSNEKHDLHVTSQQgssepVVQDLAQVVEEVIGVPQSFQKLIFKGKSlKEMETPLSALGIQDGCRVMLI 218
Cdd:cd17054     4 IKVSHGAVYHEVTVSAQA-----TFGDLKKLLVQDTGLQPQEQKLLFRGKE-KDDKDFLDLAGVKDKAKVVLV 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 157-221 2.65e-06

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 44.47  E-value: 2.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519312720 157 LHVTSQQGSSEPV-------VQDLAQVVEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLIGKK 221
Cdd:pfam00240   1 ITVKTLDGKKITLevdptdtVLELKEKIAEKEGVPPEQQRLIYSGKVLED-DQTLGEYGIEDGSTIHLVLRQ 71
PTZ00121 PTZ00121
MAEBL; Provisional
 64-138 1.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312720   64 AAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREE 138
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
PTZ00121 PTZ00121
MAEBL; Provisional
 73-291 3.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 3.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720   73 KKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEmaaaglTVTVTHSN 152
Cdd:PTZ00121  1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE------EKKKAEEA 1569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720  153 EKHDLHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLifKGKSL-KEMETPLSALGIQDGCRVMLIGKKNSPQEEVELK 231
Cdd:PTZ00121  1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAkKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720  232 KLKHLEKSVEKIADQLEELNKELTGIQQgflpkdlQAEALCKLDRRVKATIEQFMKILEE 291
Cdd:PTZ00121  1648 KAEELKKAEEENKIKAAEEAKKAEEDKK-------KAEEAKKAEEDEKKAAEALKKEAEE 1700
PTZ00121 PTZ00121
MAEBL; Provisional
 23-140 6.13e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 6.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720   23 ALRPGREPRQSEPpAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKKTRRrSTRSEELTRSEELTLSEEATWSE 102
Cdd:PTZ00121  1120 AKKKAEDARKAEE-ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED-AKKAEAARKAEEVRKAEELRKAE 1197

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1519312720  103 EATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMA 140
Cdd:PTZ00121  1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEA 1235
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
 144-218 7.48e-05

ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.


Pssm-ID: 340494 [Multi-domain]  Cd Length: 73  Bit Score: 40.62  E-value: 7.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312720 144 LTVTVTHSNekhdlHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLI 218
Cdd:cd01796     3 LTVTTEDDD-----RLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLR 72
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 2-138 1.96e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720   2 AQRGGARRPRG------DRERLGSRLRALRPGREPRQSEPPAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKK 75
Cdd:PRK12678   58 ARGGGAAAAAAtpaapaAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAA 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519312720  76 TRRRSTRSEELT-RSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREE 138
Cdd:PRK12678  138 RRGAARKAGEGGeQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD 201
PTZ00121 PTZ00121
MAEBL; Provisional
 74-146 2.15e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.15e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519312720   74 KKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMAAAGLTV 146
Cdd:PTZ00121  1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV 1187
PTZ00121 PTZ00121
MAEBL; Provisional
 67-141 2.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.79e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312720   67 ARRPRMKKKTRRrSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMAA 141
Cdd:PTZ00121  1169 ARKAEDAKKAEA-ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA 1242
PTZ00121 PTZ00121
MAEBL; Provisional
 49-138 4.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720   49 ARSTASGHDRPTRGAAAGARRPRMKKKTRRrSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEES 128
Cdd:PTZ00121  1103 AKKTETGKAEEARKAEEAKKKAEDARKAEE-ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAA 1181

                           90
                   ....*....|
gi 1519312720  129 TRSEEVTREE 138
Cdd:PTZ00121  1182 RKAEEVRKAE 1191
Ubl_NUB1 cd17062
ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, ...
 157-218 7.90e-04

ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also termed negative regulator of ubiquitin-like proteins 1, or renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1), which may function in the regulation of cell cycle progression. NUB1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif.


Pssm-ID: 340582  Cd Length: 78  Bit Score: 37.89  E-value: 7.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519312720 157 LHVTSQQGSSEPV---------VQDLAQVVEEVIGVPQSFQKLIFKGKSLKeMETPLSALGIQDGCRVMLI 218
Cdd:cd17062     7 VRLPGQGSKKKKItletslditGSELREKIAEELGVPEDRIKLISNGKVLK-DEKTLAEQGVKNNSQVMVL 76
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
 144-219 8.90e-04

ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.


Pssm-ID: 340511  Cd Length: 74  Bit Score: 37.55  E-value: 8.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519312720 144 LTVTVTHSNEKHDLHVTSqqgssEPVVQDLAQVVEEVIGVPQSFQKLI---FKGKsLKEMETPLSALGIQDGCRVMLIG 219
Cdd:cd01813     1 ITLIVKWSGKEYPVTVLS-----SDTVLDLKQRIFELTGVLPKRQKLLglkVKGK-PADDDVKLSSLKLKPNTKIMMMG 73
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 152-217 1.39e-03

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 37.65  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312720 152 NEKHDLHVTSQQgssepVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVML 217
Cdd:cd01795     5 GERKSLTVSSTT-----TLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYL 65
PTZ00121 PTZ00121
MAEBL; Provisional
 64-133 1.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.97e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720   64 AAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEE 133
Cdd:PTZ00121  1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
 147-218 2.24e-03

ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain.


Pssm-ID: 340573  Cd Length: 71  Bit Score: 36.17  E-value: 2.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519312720 147 TVTHSNEKHDLHVTSQQGSSepVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLI 218
Cdd:cd17053     2 TVNSKLLTGTVHTLQVSRST--TVAQVKAMIEDQSGVPPNEQILVYNGKRLEDGDKTLGEYGIKTGDTLYLL 71
PTZ00121 PTZ00121
MAEBL; Provisional
 20-137 2.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312720   20 RLRALRPGREPRQSEPPAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKKTRRRstRSEELTRSEELTLSEEAT 99
Cdd:PTZ00121  1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR--KAEELRKAEDARKAEAAR 1206

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1519312720  100 WSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTRE 137
Cdd:PTZ00121  1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK 1244
Ubl_UBL4A_like cd01807
ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, ...
 163-220 2.67e-03

ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, also termed GdX, is a ubiquitously expressed ubiquitin-like (Ubl) protein that forms a complex with partner proteins and participates in the protein processing through endoplasmic reticulum (ER), acting as a chaperone. As a key component of the BCL2-associated athanogene 6 (BAG6) chaperone complex, UBL4A plays a role in mediating DNA damage signaling and cell death. UBL4A also regulates insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching. Moreover, UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis. UBL4B is testis-specific, and encoded by an X-derived retrogene Ubl4b, which is specifically expressed in post-meiotic germ cells in mammals. As a germ cell-specific cytoplasmic protein, UBL4B is not present in somatic cells. Moreover, UBL4B is present in elongated spermatids, but not in spermatocytes and round spermatids, suggesting its function is restricted to late spermiogenesis. The function of UBL4A may be compensated by either UBL4B or other Ubl proteins in normal conditions. Both UBL4A and UBL4B contain a conserved Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340505 [Multi-domain]  Cd Length: 72  Bit Score: 36.19  E-value: 2.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519312720 163 QGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEmETPLSALGIQDGCRVMLIGK 220
Cdd:cd01807    16 EVSPTESVLTVKQLVAEQLNVPVSQQRLVFKGKTLAD-EHSLSDYSIGPGSKIHLVVK 72
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
 254-323 3.26e-03

BAG domain; Domain present in Hsp70 regulators.


Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 36.05  E-value: 3.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312720 254 LTGIQQGFLPKDLQAEALC------KLDRRVKATIEQFMKILEEIDTLILPENfKDSRLKRKGLVKKVQAFLAECD 323
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEgsppskKRDKEYKRLSEMLMKLLLKLDGIDTEGD-PEAREARKAAVKEVQGLLEKLD 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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