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Conserved domains on  [gi|1800051738|ref|XP_032000824|]
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putative E3 ubiquitin-protein ligase UNKL isoform X2 [Hylobates moloch]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 659-702 1.04e-19

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16772:

Pssm-ID: 473075  Cd Length: 44  Bit Score: 82.53  E-value: 1.04e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCAATAPECPYCKGQPLQW 702
Cdd:cd16772     1 KKCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCKTKILKW 44
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 25-60 1.49e-14

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


:

Pssm-ID: 375810  Cd Length: 40  Bit Score: 67.95  E-value: 1.49e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1800051738  25 YRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-610 1.72e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-------RQLALQKKEEVEAQVKQLQEELE 610
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-312 2.92e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 38.33  E-value: 2.92e-04
                          10        20
                  ....*....|....*....|....*..
gi 1800051738 286 YKSTKCNDMRQTGYCPRGPFCAFAHVE 312
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 344-484 1.44e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 344 RRDSPAEGGPKGSEQDSKQNHLAVFAAVHPPAPSMSSSVASSVASSAGSGSSSPTALPAPPARALPLGPASST------V 417
Cdd:pfam03154 142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATsqppnqT 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800051738 418 EAVLGPRSLAGSAPVAIPGSLPRAPSLHSPSSASTSPLSSLSQPLPGPVGSSAMTPpqQPPPLRSEP 484
Cdd:pfam03154 222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP--MPHSLQTGP 286
 
Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 659-702 1.04e-19

RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar proteins; UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. It shows high sequence similarity with RING finger protein unkempt (UNK), which is a metazoan-specific zinc finger protein enriched in embryonic brains, and may play a broad regulatory role during the formation of the central nervous system (CNS). UNKL contains several CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438428  Cd Length: 44  Bit Score: 82.53  E-value: 1.04e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCAATAPECPYCKGQPLQW 702
Cdd:cd16772     1 KKCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCKTKILKW 44
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 25-60 1.49e-14

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


Pssm-ID: 375810  Cd Length: 40  Bit Score: 67.95  E-value: 1.49e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1800051738  25 YRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-610 1.72e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-------RQLALQKKEEVEAQVKQLQEELE 610
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 538-668 3.16e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 45.83  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERArvadsDRQLA---LQKKEEVEAQVKQLQEELEglgv 614
Cdd:pfam04012  37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG-----NEELAreaLAEKKSLEKQAEALETQLA---- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738 615 astlpglrgcgdigtiplpKLHSLQSQLRLDLEAVDGVIFQLRAK-QCVACRERA 668
Cdd:pfam04012 108 -------------------QQRSAVEQLRKQLAALETKIQQLKAKkNLLKARLKA 143
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
659-696 5.01e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 5.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCA----ATAPECPYCK 696
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAerllRKKKKCPICR 44
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-312 2.92e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 38.33  E-value: 2.92e-04
                          10        20
                  ....*....|....*....|....*..
gi 1800051738 286 YKSTKCNDMRQTGYCPRGPFCAFAHVE 312
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 344-484 1.44e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 344 RRDSPAEGGPKGSEQDSKQNHLAVFAAVHPPAPSMSSSVASSVASSAGSGSSSPTALPAPPARALPLGPASST------V 417
Cdd:pfam03154 142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATsqppnqT 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800051738 418 EAVLGPRSLAGSAPVAIPGSLPRAPSLHSPSSASTSPLSSLSQPLPGPVGSSAMTPpqQPPPLRSEP 484
Cdd:pfam03154 222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP--MPHSLQTGP 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-612 2.44e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738  538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 612
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 539-609 2.62e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 38.99  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800051738 539 LARVRRQLDEAKRK---IRQweeswqqvkqvcDAWQREAQ---EAKERARvADSDRQLAlQKKEEVEAQVKQLQEEL 609
Cdd:PRK05759   58 QAKYEAQLAEARAEaaeIIE------------QAKKRAAQiieEAKAEAE-AEAARIKA-QAQAEIEQERKRAREEL 120
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 330-491 4.36e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 330 SPASTGSGQPGNAKRRDSPAEGGPKGSEQ-DSKQNHLAVFAAVHPPAPSMSSSVASSVASSAGSGSSSPTALPAPPARAL 408
Cdd:PRK07764  631 GAAAAPAEASAAPAPGVAAPEHHPKHVAVpDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 409 PLGPASSTVEAVLGPRSLAGSAPVAIPG-SLPRAPSLHSPSSASTSPLSSLSQPLPGPVGSSAMTPPQQPPPLRSEPGAL 487
Cdd:PRK07764  711 AGQADDPAAQPPQAAQGASAPSPAADDPvPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDA 790


                  ....
gi 1800051738 488 GSAA 491
Cdd:PRK07764  791 PSMD 794
 
Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 659-702 1.04e-19

RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar proteins; UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. It shows high sequence similarity with RING finger protein unkempt (UNK), which is a metazoan-specific zinc finger protein enriched in embryonic brains, and may play a broad regulatory role during the formation of the central nervous system (CNS). UNKL contains several CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438428  Cd Length: 44  Bit Score: 82.53  E-value: 1.04e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCAATAPECPYCKGQPLQW 702
Cdd:cd16772     1 KKCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCKTKILKW 44
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 25-60 1.49e-14

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


Pssm-ID: 375810  Cd Length: 40  Bit Score: 67.95  E-value: 1.49e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1800051738  25 YRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
RING-HC_UNK-like cd16614
RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and ...
 659-696 1.31e-13

RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and similar proteins; UNK, also known as zinc finger CCCH domain-containing protein 5, is a metazoan-specific zinc finger protein enriched in embryonic brains. It may play a broad regulatory role during the formation of the central nervous system (CNS). It is a sequence-specific RNA-binding protein required for early neuronal morphology. UNK is a neurogenic component of the mTOR pathway, and functions as a negative regulator of the timing of photoreceptor differentiation. It also specifically binds to Brg/Brm-associated factor BAF60b and promotes its ubiquitination in a Rac1-dependent manner. UNKL, also known as zinc finger CCCH domain-containing protein 5-like, is a putative E3 ubiquitin-protein ligase that may participate in a protein complex showing an E3 ligase activity regulated by RAC1. Both UNK and UNKL contain several tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438276  Cd Length: 38  Bit Score: 65.27  E-value: 1.31e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCAATAPECPYCK 696
Cdd:cd16614     1 KKCMKCEERNRSVAVLPCQHYVLCEQCAETATECPYCH 38
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-610 1.72e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-------RQLALQKKEEVEAQVKQLQEELE 610
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
538-612 2.92e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEE---SWQQVKQVCDAWQREAQEAKERARVADSDR-QLALQKKEEVEAQVKQLQEELEGL 612
Cdd:COG4717   140 ELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEA 218
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 538-668 3.16e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 45.83  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERArvadsDRQLA---LQKKEEVEAQVKQLQEELEglgv 614
Cdd:pfam04012  37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG-----NEELAreaLAEKKSLEKQAEALETQLA---- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738 615 astlpglrgcgdigtiplpKLHSLQSQLRLDLEAVDGVIFQLRAK-QCVACRERA 668
Cdd:pfam04012 108 -------------------QQRSAVEQLRKQLAALETKIQQLKAKkNLLKARLKA 143
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
538-612 4.03e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 45.20  E-value: 4.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARvaDSDRQLALQKKEEVEAQVKQLQEELEGL 612
Cdd:COG1842    38 DLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGR--EDLAREALERKAELEAQAEALEAQLAQL 110
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
659-696 5.01e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 5.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCA----ATAPECPYCK 696
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAerllRKKKKCPICR 44
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-612 1.08e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 612
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-612 1.58e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738 538 ELARVRRQLDEAKRKIrqwEESWQQVKQVcdawQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 612
Cdd:COG4372    60 ELEQLEEELEQARSEL---EQLEEELEEL----NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-612 2.00e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.00e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800051738  538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADS---DRQLALQKKEEVEAQV-KQLQEELEGL 612
Cdd:COG4913    700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVERELrENLEERIDAL 778
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
 661-698 2.25e-04

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438178 [Multi-domain]  Cd Length: 48  Bit Score: 39.20  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1800051738 661 CVACRERAHGAVLQPCQHHVLCEPCAATAPECPYCKGQ 698
Cdd:cd16515     4 CVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRAD 41
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 538-610 2.56e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.06  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQV---KQVCDAWQREAQEAKER-----ARVADSDRQLALQ---KKEEV-------- 598
Cdd:pfam20492  21 ETKKAQEELEESEETAEELEEERRQAeeeAERLEQKRQEAEEEKERleesaEMEAEEKEQLEAElaeAQEEIarleeeve 100

                          90
                  ....*....|....
gi 1800051738 599 --EAQVKQLQEELE 610
Cdd:pfam20492 101 rkEEEARRLQEELE 114
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-312 2.92e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 38.33  E-value: 2.92e-04
                          10        20
                  ....*....|....*....|....*..
gi 1800051738 286 YKSTKCNDMRQTGYCPRGPFCAFAHVE 312
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
DUF2058 pfam09831
Uncharacterized protein conserved in bacteria (DUF2058); This domain, found in various ...
 547-608 3.97e-04

Uncharacterized protein conserved in bacteria (DUF2058); This domain, found in various prokaryotic proteins, has no known function.


Pssm-ID: 430862 [Multi-domain]  Cd Length: 174  Bit Score: 41.80  E-value: 3.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800051738 547 DEAK-RKIRQweESWQQVKQ-----VCDAWQREAQEAkeRARVADSDRQLALQKKEEVE-----AQVKQLQEE 608
Cdd:pfam09831  13 DKKKaKQAKK--EKRKQRKQkrkkgAVDEAKAAAEEA--KAEKAERDRELNRQRQAEAEqkalaAQIRQLIEQ 81
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
 658-697 4.42e-04

RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed in cancer and associated with tumor cell survival, chemoresistance, disease progression, and poor prognosis. They function primarily as negative regulators of cell death. They regulate caspases and apoptosis through the inhibition of specific members of the caspase family of cysteine proteases. In addition, IAPs has been implicated in a multitude of other cellular processes, including inflammatory signalling and immunity, mitogenic kinase signalling, proliferation and mitosis, as well as cell invasion and metastasis. IAPs in this family includes cellular inhibitor of apoptosis protein c-IAP1 (BIRC2) and c-IAP2 (BIRC3), XIAP (BIRC4), BIRC7, and BIRC8, all of which contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of polyubiquitin (polyUb), and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. The UBA domain is only absent in mammalian homologs of BIRC7. Moreover, c-IAPs contains an additional caspase activation and recruitment domain (CARD) between the UBA and C3HC4-type RING-HC domains. The CARD domain may serve as a protein interaction surface.


Pssm-ID: 438173 [Multi-domain]  Cd Length: 40  Bit Score: 38.39  E-value: 4.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800051738 658 AKQCVACRERAHGAVLQPCQHHVLCEPCAATAPECPYCKG 697
Cdd:cd16510     1 EKLCKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-614 5.00e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEA-KERARVADSDRQLALQKK-------------EEVEAQVK 603
Cdd:COG4372    81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqKERQDLEQQRKQLEAQIAelqseiaereeelKELEEQLE 160

                          90
                  ....*....|.
gi 1800051738 604 QLQEELEGLGV 614
Cdd:COG4372   161 SLQEELAALEQ 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-612 7.73e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738  538 ELARVRRQLDEAKRKIRQ----------WEESWQQ------VKQVCDAW--QREAQEAKERARVADSDRQLALQKKEEVE 599
Cdd:COG4913    236 DLERAHEALEDAREQIELlepirelaerYAAARERlaeleyLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLE 315

                           90
                   ....*....|...
gi 1800051738  600 AQVKQLQEELEGL 612
Cdd:COG4913    316 ARLDALREELDEL 328
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-610 7.80e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.80e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1800051738  538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-RQLALQKKEEVEAQVKQLQEELE 610
Cdd:COG4913    282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELE 355
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
 661-695 9.11e-04

RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, also known as zinc finger CCCH domain-containing protein 5, is a metazoan-specific zinc finger protein enriched in embryonic brains. It may play a broad regulatory role during the formation of the central nervous system (CNS). It is a sequence-specific RNA-binding protein required for early neuronal morphology. UNK is a neurogenic component of the mTOR pathway, and functions as a negative regulator of the timing of photoreceptor differentiation. It also specifically binds to Brg/Brm-associated factor BAF60b and promotes its ubiquitination in a Rac1-dependent manner. UNK contains six tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438427  Cd Length: 42  Bit Score: 37.50  E-value: 9.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1800051738 661 CVACRERahGAVLQPCQHHVLCEPCaATAPECPYC 695
Cdd:cd16771     5 CLKCQEL--KRVTLPCQHALLCETC-ATSEECPIC 36
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
539-660 1.08e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738  539 LARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLAlqkkeEVEAQVKQLQEELEGLGVAStl 618
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASS-- 684

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1800051738  619 pglrgcgdigtiplPKLHSLQSQL---RLDLEAVDGVIFQLRAKQ 660
Cdd:COG4913    685 --------------DDLAALEEQLeelEAELEELEEELDELKGEI 715
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-612 1.25e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738  538 ELARVRRQLDEAKRKIRQWEESWQQVKQVC-----------DAWQREAQEAKERARVADSDRQL-------ALQKKEEVE 599
Cdd:COG4913    339 RLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEAleealaeAEAALRDLR 418

                           90
                   ....*....|...
gi 1800051738  600 AQVKQLQEELEGL 612
Cdd:COG4913    419 RELRELEAEIASL 431
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 344-484 1.44e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 344 RRDSPAEGGPKGSEQDSKQNHLAVFAAVHPPAPSMSSSVASSVASSAGSGSSSPTALPAPPARALPLGPASST------V 417
Cdd:pfam03154 142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATsqppnqT 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800051738 418 EAVLGPRSLAGSAPVAIPGSLPRAPSLHSPSSASTSPLSSLSQPLPGPVGSSAMTPpqQPPPLRSEP 484
Cdd:pfam03154 222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP--MPHSLQTGP 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
538-615 1.71e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQL------------ALQKKEEVEAQVKQL 605
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreLEEELEELEAELAEL 175

                          90
                  ....*....|....
gi 1800051738 606 QEE----LEGLGVA 615
Cdd:COG4717   176 QEEleelLEQLSLA 189
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-612 2.44e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738  538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 612
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-612 2.53e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 612
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-610 2.55e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELE 610
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 539-609 2.62e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 38.99  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800051738 539 LARVRRQLDEAKRK---IRQweeswqqvkqvcDAWQREAQ---EAKERARvADSDRQLAlQKKEEVEAQVKQLQEEL 609
Cdd:PRK05759   58 QAKYEAQLAEARAEaaeIIE------------QAKKRAAQiieEAKAEAE-AEAARIKA-QAQAEIEQERKRAREEL 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-660 3.02e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738  538 ELARVRRQLDEAKRKIRQWEESWQQVKQvcDAWQREAQEAKERARVadsdrQLALQKKEEVEAQVKQLQEELEGLGVAST 617
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRS--KVAQLELQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLKKLE 431

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1800051738  618 LPGLRGC-GDIGTIPlPKLHSLQSQLRLDLEAVDGVIFQLRAKQ 660
Cdd:TIGR02168  432 EAELKELqAELEELE-EELEELQEELERLEEALEELREELEEAE 474
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
 657-697 3.32e-03

RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and similar proteins; This subfamily includes Arabidopsis thaliana MIP1, RING finger protein 4 (RF4) and RING finger protein 298 (RF298). MIP1 interacts with MND1, HOP2 and XRI1. RF4 and RF298 are putative E3 ubiquitin-protein ligase that may mediate E2-dependent protein ubiquitination. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438490 [Multi-domain]  Cd Length: 55  Bit Score: 36.33  E-value: 3.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1800051738 657 RAKQCVACRERAHGAVLQPCQHHVLCEPCA-----ATAPECPYCKG 697
Cdd:cd23128     2 RERECVMCMEEERSVVFLPCAHQVVCSGCNdlhekKGMRECPSCRG 47
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
 657-695 3.39e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also known as baculoviral IAP repeat-containing protein 4 (BIRC4), IAP-like protein (ILP), inhibitor of apoptosis protein 3 (IAP-3), or X-linked inhibitor of apoptosis protein (X-linked IAP), is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases, including caspase-3, -7, and -9. It promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. The ubiquitin-protein ligase (E3) activity of XIAP also exhibits in the ubiquitination of second mitochondria-derived activator of caspases (Smac). The mitochondrial proteins, Smac/DIABLO and Omi/HtrA2, can inhibit the antiapoptotic activity of XIAP. XIAP has also been implicated in several intracellular signaling cascades involved in the cellular response to stress, such as the c-Jun N-terminal kinase (JNK), the nuclear factor-kappaB (NF-kappaB), and the transforming growth factor-beta (TGF-beta) pathways. Moreover, XIAP can regulate copper homeostasis by interacting with MURR1. BIRC8, also known as inhibitor of apoptosis-like protein 2, IAP-like protein 2, ILP-2, or testis-specific inhibitor of apoptosis, is a tissue-specific homolog of E3 ubiquitin-protein ligase XIAP. It has been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. Both XIAP and BIRC8 contain three N-terminal baculoviral IAP repeat (BIR) domains, a ubiquitin-association (UBA) domain and a C3HC4-type RING-HC finger at the carboxyl terminus.


Pssm-ID: 438374 [Multi-domain]  Cd Length: 64  Bit Score: 36.66  E-value: 3.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1800051738 657 RAKQCVACRERAHGAVLQPCQHHVLCEPCAATAPECPYC 695
Cdd:cd16714    13 EEKLCKICMDRNISIVFIPCGHLVTCKQCAEALDKCPIC 51
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
538-612 3.52e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQV---CDAWQREAQEAKERARVADSDRQL--ALQKKEEVEAQVKQLQEELEGL 612
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEEL 151
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 330-491 4.36e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 330 SPASTGSGQPGNAKRRDSPAEGGPKGSEQ-DSKQNHLAVFAAVHPPAPSMSSSVASSVASSAGSGSSSPTALPAPPARAL 408
Cdd:PRK07764  631 GAAAAPAEASAAPAPGVAAPEHHPKHVAVpDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 409 PLGPASSTVEAVLGPRSLAGSAPVAIPG-SLPRAPSLHSPSSASTSPLSSLSQPLPGPVGSSAMTPPQQPPPLRSEPGAL 487
Cdd:PRK07764  711 AGQADDPAAQPPQAAQGASAPSPAADDPvPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDA 790


                  ....
gi 1800051738 488 GSAA 491
Cdd:PRK07764  791 PSMD 794
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 659-696 5.11e-03

Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 (CGRRF1), RNF156 (MGRN1), RNF157 and similar proteins; This subfamily corresponds to a group of RING finger proteins containing a modified C3HC5-type RING-HC finger, which is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. Cell growth regulator with RING finger domain protein 1 (CGRRF1), also known as cell growth regulatory gene 19 protein (CGR19) or RING finger protein 197 (RNF197), functions as a novel biomarker to monitor endometrial sensitivity and response to insulin-sensitizing drugs, such as metformin, in the context of obesity. RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Mahogunin ring finger-1 (MGRN1), also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in the brain. It is a homolog of the E3 ligase MGRN1. In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis.


Pssm-ID: 438311 [Multi-domain]  Cd Length: 40  Bit Score: 35.38  E-value: 5.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800051738 659 KQCVACRERAHGAVLQPCQHHVLCEPCAATA--PECPYCK 696
Cdd:cd16649     1 GLCVVCLENPASVLLLPCRHLCLCEVCAKGLrgKTCPICR 40
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 538-612 6.64e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 6.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQV---KQVcDAWQREAQEAKERARVADsDRQLALQKK-EEVEAQVKQLQEELEGL 612
Cdd:COG1579    60 EIKRLELEIEEVEARIKKYEEQLGNVrnnKEY-EALQKEIESLKRRISDLE-DEILELMERiEELEEELAELEAELAEL 136
RING-HC_MEX3C cd16722
RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger ...
 661-701 7.50e-03

RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger and KH domain-containing protein 2 (RKHD2), or RING finger protein 194 (RNF194), is an RNA-binding phosphoprotein that acts as a suppressor of chromosomal instability. It functions as an ubiquitin E3 ligase responsible for the post-transcriptional, HLA-A allotype-specific regulation of MHC class I molecules (MHC-I). It also modifies retinoic acid inducible gene-1 (RIG-I) in stress granules and plays a critical role in eliciting antiviral immune responses. Moreover, MEX3C plays an essential role in normal postnatal growth via enhancing the local expression of insulin-like growth factor 1 (IGF1) in bone. It may also be involved in metabolic regulation of energy balance. MEX3C contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3C shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438382 [Multi-domain]  Cd Length: 55  Bit Score: 35.34  E-value: 7.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1800051738 661 CVACRERAHGAVLQPCQHHVLCEPCA-----ATAPECPYCKG---QPLQ 701
Cdd:cd16722     4 CVICFENEVIAALVPCGHNLFCMECAnkiceKETPSCPVCQTavtQAIQ 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 329-496 7.59e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 329 TSPASTGSGQPGNAKRRDSPA----------EGGPKGSEQDSKQNHLAVFAAVHPPAPS-MSSSVASSVASSAGSGSSSP 397
Cdd:PRK07764  599 GPPAPASSGPPEEAARPAAPAapaapaapapAGAAAAPAEASAAPAPGVAAPEHHPKHVaVPDASDGGDGWPAKAGGAAP 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 398 TALPAPPARALPLGPAS-STVEAVLGPRSLAGSAPVAIPGSLPRAPSLHSPSSASTSPLSSLSQPLPGPVGSSAMTPPQQ 476
Cdd:PRK07764  679 AAPPPAPAPAAPAAPAGaAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758

                         170       180
                  ....*....|....*....|
gi 1800051738 477 PPPLRSEPGALGSAASSYSP 496
Cdd:PRK07764  759 PPPPAPAPAAAPAAAPPPSP 778
fliH PRK06669
flagellar assembly protein H; Validated
 538-610 7.79e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 38.84  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 538 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD---------RQLALQKKEEVEAQVKQLQEE 608
Cdd:PRK06669   21 EIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEiveaaeeeaKEELLKKTDEASSIIEKLQMQ 100


                  ..
gi 1800051738 609 LE 610
Cdd:PRK06669  101 IE 102
RING-HC_MEX3A cd16720
RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger ...
 658-695 8.36e-03

RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger and KH domain-containing protein 4 (RKHD4), is an RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It has been implicated in the regulation of tumorigenesis. It controls the polarity and stemness of intestinal epithelial cells through the post-transcriptional regulation of the homeobox transcription factor CDX2, which plays a crucial role in intestinal cell fate specification, both during normal development and in tumorigenic processes involving intestinal reprogramming. Moreover, it exhibits a transforming activity when overexpressed in gastric epithelial cells. MEX3A contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3A shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438380 [Multi-domain]  Cd Length: 56  Bit Score: 35.32  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1800051738 658 AKQCVACRERAHGAVLQPCQHHVLCEPCAA-----TAPECPYC 695
Cdd:cd16720     2 GRDCMVCFESEVTAALVPCGHNLFCMECAVricerNEPECPVC 44
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 345-488 8.50e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.31  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738 345 RDSPAEGGPKGSEQDSKQNHLAVFAAVHPPAPSmsssvassvASSAGSGSSSPTALPAPPARALPLGPASSTVEAVLGPr 424
Cdd:PRK14951  365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQA---------AAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAP- 434

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1800051738 425 slaGSAPVAIPGSLPRAPSLHSPSSASTSPLSSLSQPLPGPVgSSAMTPPQQPPPLRSEPGALG 488
Cdd:PRK14951  435 ---AAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVA-SAAPAPAAAPAAARLTPTEEG 494
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-612 8.53e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800051738  538 ELARVRRQLDEAKRKIRQW--EESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQ--------VKQLQE 607
Cdd:COG4913    266 AARERLAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLER 345


                   ....*
gi 1800051738  608 ELEGL 612
Cdd:COG4913    346 EIERL 350
 
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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