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Conserved domains on  [gi|6322791|ref|NP_012864|]
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cleavage polyadenylation factor subunit MPE1 [Saccharomyces cerevisiae S288C]

Protein Classification

RING finger protein( domain architecture ID 11474170)

RING finger protein may function as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination

CATH:  4.10.60.10
Gene Ontology:  GO:0008270|GO:0016567|GO:0004842|GO:0006397|GO:0061630
PubMed:  19489725|11007473|8317827
SCOP:  3000160

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1-441 0e+00

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


:

Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 702.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791    1 MSSTIFYRFKSQRNTSRILFDGTGLTVFDLKREIIQENKLGDGTDFQLKIYNPDTEEEYDDDAFVIPRSTSVIVKRSPAI 80
Cdd:COG5222   1 MSSVINYRFKSQKNFSRISFDGTGLPVFDLKREIINQRKLGSGKDFDLLFYNGETNEEYDDDYFVIPRSTSVIVSRIPAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791   81 KSFSVHSRLKGnvGAAALGNATRYVTGRPRVLQKRQHTATTTANVSGTTEEERIASMFATQENQWEQTQEEMSAATPVFF 160
Cdd:COG5222  81 KSKGTAARYKG--GAPKTTGARGYNVKRPRMLQKKAPITSGELNSQSSSEDAAIQQMFQVSSDQWRETQDKMSSATPIYK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  161 KSQTnKNSAQENEGPPPPGYMCYRCGGRDHWIKNCPTNSDPNFEGKRIRRTTGIPKKFLKSIEIdpetmtPEEMAQRKIM 240
Cdd:COG5222 159 PNQH-RIGAQKHNKPPPPGYVCYRCGQKGHWIQNCPTNQDPNFDGKRIRRTTGIPKDFLKPVEG------PNEPSNAAIM 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  241 ITDEGKFVVQVEDKQSWEDYQRKRENRQIDGDEtIWrKGHFKDLPddLKCPLTGGLLRQPVKTsKCCNIDFSKEALENAL 320
Cdd:COG5222 232 ITPEGGYVVAQPDVQSWEKYQQRTKAVAEIPDQ-VY-KMQPPNIS--LKCPLCHCLLRNPMKT-PCCGHTFCDECIGTAL 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  321 VESDFVCPNCETRDILLDSLVPDQDKEKEVETFLKKQEELHGSSKDGNQPETKKMKLMDPTGTAGLNNNTSLPTSVNNGG 400
Cdd:COG5222 307 LDSDFKCPNCSRKDVLLDGLTPDIDKKLEVEKALKKQRKKVGTSDDNNTPMSEKRKREDPNSSAVFSKATAEPAFKSAMA 386

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 6322791  401 TPVPPVPLPFGIPPFPMFPMPFMPPTATITNPHQADASPKK 441
Cdd:COG5222 387 IPMPSMPHVQGFPPFPMMPLPQMPPMMMIANPPRTNSRPSN 427
 
Name Accession Description Interval E-value
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1-441 0e+00

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 702.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791    1 MSSTIFYRFKSQRNTSRILFDGTGLTVFDLKREIIQENKLGDGTDFQLKIYNPDTEEEYDDDAFVIPRSTSVIVKRSPAI 80
Cdd:COG5222   1 MSSVINYRFKSQKNFSRISFDGTGLPVFDLKREIINQRKLGSGKDFDLLFYNGETNEEYDDDYFVIPRSTSVIVSRIPAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791   81 KSFSVHSRLKGnvGAAALGNATRYVTGRPRVLQKRQHTATTTANVSGTTEEERIASMFATQENQWEQTQEEMSAATPVFF 160
Cdd:COG5222  81 KSKGTAARYKG--GAPKTTGARGYNVKRPRMLQKKAPITSGELNSQSSSEDAAIQQMFQVSSDQWRETQDKMSSATPIYK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  161 KSQTnKNSAQENEGPPPPGYMCYRCGGRDHWIKNCPTNSDPNFEGKRIRRTTGIPKKFLKSIEIdpetmtPEEMAQRKIM 240
Cdd:COG5222 159 PNQH-RIGAQKHNKPPPPGYVCYRCGQKGHWIQNCPTNQDPNFDGKRIRRTTGIPKDFLKPVEG------PNEPSNAAIM 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  241 ITDEGKFVVQVEDKQSWEDYQRKRENRQIDGDEtIWrKGHFKDLPddLKCPLTGGLLRQPVKTsKCCNIDFSKEALENAL 320
Cdd:COG5222 232 ITPEGGYVVAQPDVQSWEKYQQRTKAVAEIPDQ-VY-KMQPPNIS--LKCPLCHCLLRNPMKT-PCCGHTFCDECIGTAL 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  321 VESDFVCPNCETRDILLDSLVPDQDKEKEVETFLKKQEELHGSSKDGNQPETKKMKLMDPTGTAGLNNNTSLPTSVNNGG 400
Cdd:COG5222 307 LDSDFKCPNCSRKDVLLDGLTPDIDKKLEVEKALKKQRKKVGTSDDNNTPMSEKRKREDPNSSAVFSKATAEPAFKSAMA 386

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 6322791  401 TPVPPVPLPFGIPPFPMFPMPFMPPTATITNPHQADASPKK 441
Cdd:COG5222 387 IPMPSMPHVQGFPPFPMMPLPQMPPMMMIANPPRTNSRPSN 427
DWNN pfam08783
DWNN domain; DWNN is a ubiquitin like domain found at the N terminus of the RBBP6 family of ...
 5-78 1.59e-41

DWNN domain; DWNN is a ubiquitin like domain found at the N terminus of the RBBP6 family of splicing-associated proteins. The DWNN domain is independently expressed in higher vertebrates so it may function as a novel ubiquitin-like modifier of other proteins.


Pssm-ID: 462603  Cd Length: 74  Bit Score: 141.83  E-value: 1.59e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322791      5 IFYRFKSQRNTSRILFDGTGLTVFDLKREIIQENKLGDGTDFQLKIYNPDTEEEYDDDAFVIPRSTSVIVKRSP 78
Cdd:pfam08783   1 VYYKFKSQKDYSRITFDGTGISVFDLKREIILQKKLGKGTDFDLLIYNAQTNEEYKDDTTLIPRNTSVIVRRVP 74
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 285-340 8.04e-12

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 60.11  E-value: 8.04e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322791  285 PDDLKCPLTGGLLRQPVKTsKCCNIDFSKEALENALVESDFVCPNCETRDILLDSL 340
Cdd:cd16620   1 PDELKCPICKDLMKDAVLT-PCCGNSFCDECIRTALLEEDFTCPTCKEPDVSPDAL 55
ZnF_C2HC smart00343
zinc finger;
182-196 1.12e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 1.12e-03
                           10
                   ....*....|....*
gi 6322791     182 CYRCGGRDHWIKNCP 196
Cdd:smart00343   2 CYNCGKEGHIARDCP 16
 
Name Accession Description Interval E-value
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1-441 0e+00

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 702.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791    1 MSSTIFYRFKSQRNTSRILFDGTGLTVFDLKREIIQENKLGDGTDFQLKIYNPDTEEEYDDDAFVIPRSTSVIVKRSPAI 80
Cdd:COG5222   1 MSSVINYRFKSQKNFSRISFDGTGLPVFDLKREIINQRKLGSGKDFDLLFYNGETNEEYDDDYFVIPRSTSVIVSRIPAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791   81 KSFSVHSRLKGnvGAAALGNATRYVTGRPRVLQKRQHTATTTANVSGTTEEERIASMFATQENQWEQTQEEMSAATPVFF 160
Cdd:COG5222  81 KSKGTAARYKG--GAPKTTGARGYNVKRPRMLQKKAPITSGELNSQSSSEDAAIQQMFQVSSDQWRETQDKMSSATPIYK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  161 KSQTnKNSAQENEGPPPPGYMCYRCGGRDHWIKNCPTNSDPNFEGKRIRRTTGIPKKFLKSIEIdpetmtPEEMAQRKIM 240
Cdd:COG5222 159 PNQH-RIGAQKHNKPPPPGYVCYRCGQKGHWIQNCPTNQDPNFDGKRIRRTTGIPKDFLKPVEG------PNEPSNAAIM 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  241 ITDEGKFVVQVEDKQSWEDYQRKRENRQIDGDEtIWrKGHFKDLPddLKCPLTGGLLRQPVKTsKCCNIDFSKEALENAL 320
Cdd:COG5222 232 ITPEGGYVVAQPDVQSWEKYQQRTKAVAEIPDQ-VY-KMQPPNIS--LKCPLCHCLLRNPMKT-PCCGHTFCDECIGTAL 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322791  321 VESDFVCPNCETRDILLDSLVPDQDKEKEVETFLKKQEELHGSSKDGNQPETKKMKLMDPTGTAGLNNNTSLPTSVNNGG 400
Cdd:COG5222 307 LDSDFKCPNCSRKDVLLDGLTPDIDKKLEVEKALKKQRKKVGTSDDNNTPMSEKRKREDPNSSAVFSKATAEPAFKSAMA 386

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 6322791  401 TPVPPVPLPFGIPPFPMFPMPFMPPTATITNPHQADASPKK 441
Cdd:COG5222 387 IPMPSMPHVQGFPPFPMMPLPQMPPMMMIANPPRTNSRPSN 427
DWNN pfam08783
DWNN domain; DWNN is a ubiquitin like domain found at the N terminus of the RBBP6 family of ...
 5-78 1.59e-41

DWNN domain; DWNN is a ubiquitin like domain found at the N terminus of the RBBP6 family of splicing-associated proteins. The DWNN domain is independently expressed in higher vertebrates so it may function as a novel ubiquitin-like modifier of other proteins.


Pssm-ID: 462603  Cd Length: 74  Bit Score: 141.83  E-value: 1.59e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322791      5 IFYRFKSQRNTSRILFDGTGLTVFDLKREIIQENKLGDGTDFQLKIYNPDTEEEYDDDAFVIPRSTSVIVKRSP 78
Cdd:pfam08783   1 VYYKFKSQKDYSRITFDGTGISVFDLKREIILQKKLGKGTDFDLLIYNAQTNEEYKDDTTLIPRNTSVIVRRVP 74
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 285-340 8.04e-12

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 60.11  E-value: 8.04e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322791  285 PDDLKCPLTGGLLRQPVKTsKCCNIDFSKEALENALVESDFVCPNCETRDILLDSL 340
Cdd:cd16620   1 PDELKCPICKDLMKDAVLT-PCCGNSFCDECIRTALLEEDFTCPTCKEPDVSPDAL 55
zf-CCHC_2 pfam13696
Zinc knuckle; This is a zinc-binding domain of the form CxxCxxxGHxxxxC from a variety of ...
 177-197 8.60e-07

Zinc knuckle; This is a zinc-binding domain of the form CxxCxxxGHxxxxC from a variety of different species.


Pssm-ID: 463959 [Multi-domain]  Cd Length: 21  Bit Score: 44.81  E-value: 8.60e-07
                          10        20
                  ....*....|....*....|.
gi 6322791    177 PPGYMCYRCGGRDHWIKNCPT 197
Cdd:pfam13696   1 PPGYVCHICGKKGHYIQDCPT 21
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 288-351 3.86e-05

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 41.48  E-value: 3.86e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322791  288 LKCPLTGGLLRQPVKTSKCCNIdFSKEALENALVESD--FVCP--NCeTRDILLDSLVPDQDKEKEVE 351
Cdd:cd16651   1 LKCPITQQLMVDPVRNKKCGHT-YEKAAILQYLQSRKkkAKCPvaGC-RNTVSKSDLVPDPELKRRIE 66
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
 287-328 1.03e-03

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 37.27  E-value: 1.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6322791    287 DLKCPLTGGLLRQPVkTSKCCNIDFSKEALENALVESDFV-CP 328
Cdd:pfam11789  11 SLTCPLTLQPFVEPV-TSKKCNHVFEKDAILEMLKRNPTVkCP 52
ZnF_C2HC smart00343
zinc finger;
182-196 1.12e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.27  E-value: 1.12e-03
                           10
                   ....*....|....*
gi 6322791     182 CYRCGGRDHWIKNCP 196
Cdd:smart00343   2 CYNCGKEGHIARDCP 16
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
 288-330 4.15e-03

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 34.92  E-value: 4.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6322791  288 LKCPLTGGLLRQPVKTSKC--CnidFSKEALENALVESD--FVCPNC 330
Cdd:cd16452   1 LKCPITQKRMKDPVRGKHCghC---FDLEAILQYLKRRKkkWKCPVC 44
 
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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