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Conserved domains on  [gi|1722504626|ref|NP_001359036|]
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putative E3 ubiquitin-protein ligase UNKL isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 690-733 5.88e-20

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: 83.30  E-value: 5.88e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKGQPLQW 733
Cdd:cd16772     1 KKCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCKTKILKW 44
zf_CCCH_5 super family cl39722
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 25-60 6.10e-15

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.


The actual alignment was detected with superfamily member pfam18384:

Pssm-ID: 375810  Cd Length: 40  Bit Score: 69.11  E-value: 6.10e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1722504626  25 YRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
569-641 1.82e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-------RQLALQKKEEVEAQVKQLQEELE 641
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-312 2.22e-04

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


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 38.71  E-value: 2.22e-04
                          10        20
                  ....*....|....*....|....*..
gi 1722504626 286 YKSTKCNDMRQTGYCPRGPFCAFAHVE 312
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
 
Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 690-733 5.88e-20

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: 83.30  E-value: 5.88e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKGQPLQW 733
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 6.10e-15

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: 69.11  E-value: 6.10e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1722504626  25 YRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
569-641 1.82e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-------RQLALQKKEEVEAQVKQLQEELE 641
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 569-699 3.33e-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: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERArvadsDRQLA---LQKKEEVEAQVKQLQEELEglgv 645
Cdd:pfam04012  37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG-----NEELAreaLAEKKSLEKQAEALETQLA---- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626 646 astlpglrgcgdigtiplpKLHSLQSQLRLDLEAVDGVIFQLRAK-QCVACRERA 699
Cdd:pfam04012 108 -------------------QQRSAVEQLRKQLAALETKIQQLKAKkNLLKARLKA 143
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
690-727 5.66e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 5.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCA----ATAPECPYCK 727
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAerllRKKKKCPICR 44
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-312 2.22e-04

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 38.71  E-value: 2.22e-04
                          10        20
                  ....*....|....*....|....*..
gi 1722504626 286 YKSTKCNDMRQTGYCPRGPFCAFAHVE 312
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
570-713 8.98e-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: 8.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626  570 LARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLAlqkkeEVEAQVKQLQEELEGLgvastl 649
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERL------ 680

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722504626  650 pgLRGCGDIGTIP--LPKLHSLQSQLRLDLEAVDGVIFQLRAK------QCVACRERAHGAVLRPCQHHILC 713
Cdd:COG4913    681 --DASSDDLAALEeqLEELEAELEELEEELDELKGEIGRLEKEleqaeeELDELQDRLEAAEDLARLELRAL 750
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 569-643 2.58e-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: 2.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626  569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 643
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 570-640 2.75e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 38.99  E-value: 2.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722504626 570 LARVRRQLDEAKRK---IRQweeswqqvkqvcDAWQREAQ---EAKERARvADSDRQLAlQKKEEVEAQVKQLQEEL 640
Cdd:PRK05759   58 QAKYEAQLAEARAEaaeIIE------------QAKKRAAQiieEAKAEAE-AEAARIKA-QAQAEIEQERKRAREEL 120
 
Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 690-733 5.88e-20

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: 83.30  E-value: 5.88e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKGQPLQW 733
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 6.10e-15

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: 69.11  E-value: 6.10e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1722504626  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 ...
 690-727 3.04e-14

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: 67.20  E-value: 3.04e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCK 727
Cdd:cd16614     1 KKCMKCEERNRSVAVLPCQHYVLCEQCAETATECPYCH 38
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
569-641 1.82e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-------RQLALQKKEEVEAQVKQLQEELE 641
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
569-643 3.09e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 3.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEE---SWQQVKQVCDAWQREAQEAKERARVADSDR-QLALQKKEEVEAQVKQLQEELEGL 643
Cdd:COG4717   140 ELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEA 218
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 569-699 3.33e-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: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERArvadsDRQLA---LQKKEEVEAQVKQLQEELEglgv 645
Cdd:pfam04012  37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG-----NEELAreaLAEKKSLEKQAEALETQLA---- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626 646 astlpglrgcgdigtiplpKLHSLQSQLRLDLEAVDGVIFQLRAK-QCVACRERA 699
Cdd:pfam04012 108 -------------------QQRSAVEQLRKQLAALETKIQQLKAKkNLLKARLKA 143
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
569-643 4.24e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 45.20  E-value: 4.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARvaDSDRQLALQKKEEVEAQVKQLQEELEGL 643
Cdd:COG1842    38 DLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGR--EDLAREALERKAELEAQAEALEAQLAQL 110
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
690-727 5.66e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 5.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCA----ATAPECPYCK 727
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAerllRKKKKCPICR 44
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
569-643 1.14e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 643
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
569-643 1.67e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626 569 ELARVRRQLDEAKRKIrqwEESWQQVKQVcdawQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 643
Cdd:COG4372    60 ELEQLEEELEQARSEL---EQLEEELEEL----NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
569-643 2.11e-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: 2.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722504626  569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADS---DRQLALQKKEEVEAQV-KQLQEELEGL 643
Cdd:COG4913    700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVERELrENLEERIDAL 778
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-312 2.22e-04

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 38.71  E-value: 2.22e-04
                          10        20
                  ....*....|....*....|....*..
gi 1722504626 286 YKSTKCNDMRQTGYCPRGPFCAFAHVE 312
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
 692-729 2.24e-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: 2.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1722504626 692 CVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKGQ 729
Cdd:cd16515     4 CVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRAD 41
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 569-641 2.43e-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: 41.44  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQV---KQVCDAWQREAQEAKER-----ARVADSDRQLALQ---KKEEV-------- 629
Cdd:pfam20492  21 ETKKAQEELEESEETAEELEEERRQAeeeAERLEQKRQEAEEEKERleesaEMEAEEKEQLEAElaeAQEEIarleeeve 100

                          90
                  ....*....|....
gi 1722504626 630 --EAQVKQLQEELE 641
Cdd:pfam20492 101 rkEEEARRLQEELE 114
DUF2058 pfam09831
Uncharacterized protein conserved in bacteria (DUF2058); This domain, found in various ...
 578-639 4.18e-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: 4.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1722504626 578 DEAK-RKIRQweESWQQVKQ-----VCDAWQREAQEAkeRARVADSDRQLALQKKEEVE-----AQVKQLQEE 639
Cdd:pfam09831  13 DKKKaKQAKK--EKRKQRKQkrkkgAVDEAKAAAEEA--KAEKAERDRELNRQRQAEAEqkalaAQIRQLIEQ 81
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
569-645 5.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEA-KERARVADSDRQLALQKK-------------EEVEAQVK 634
Cdd:COG4372    81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqKERQDLEQQRKQLEAQIAelqseiaereeelKELEEQLE 160

                          90
                  ....*....|.
gi 1722504626 635 QLQEELEGLGV 645
Cdd:COG4372   161 SLQEELAALEQ 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
569-643 8.18e-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: 8.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626  569 ELARVRRQLDEAKRKIRQ----------WEESWQQ------VKQVCDAW--QREAQEAKERARVADSDRQLALQKKEEVE 630
Cdd:COG4913    236 DLERAHEALEDAREQIELlepirelaerYAAARERlaeleyLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLE 315

                           90
                   ....*....|...
gi 1722504626  631 AQVKQLQEELEGL 643
Cdd:COG4913    316 ARLDALREELDEL 328
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
569-641 8.25e-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: 8.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722504626  569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD-RQLALQKKEEVEAQVKQLQEELE 641
Cdd:COG4913    282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELE 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
570-713 8.98e-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: 8.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626  570 LARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLAlqkkeEVEAQVKQLQEELEGLgvastl 649
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERL------ 680

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722504626  650 pgLRGCGDIGTIP--LPKLHSLQSQLRLDLEAVDGVIFQLRAK------QCVACRERAHGAVLRPCQHHILC 713
Cdd:COG4913    681 --DASSDDLAALEeqLEELEAELEELEEELDELKGEIGRLEKEleqaeeELDELQDRLEAAEDLARLELRAL 750
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
 692-726 1.02e-03

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: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1722504626 692 CVACRERahGAVLRPCQHHILCEPCaATAPECPYC 726
Cdd:cd16771     5 CLKCQEL--KRVTLPCQHALLCETC-ATSEECPIC 36
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
569-643 1.32e-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: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626  569 ELARVRRQLDEAKRKIRQWEESWQQVKQVC-----------DAWQREAQEAKERARVADSDRQL-------ALQKKEEVE 630
Cdd:COG4913    339 RLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEAleealaeAEAALRDLR 418

                           90
                   ....*....|...
gi 1722504626  631 AQVKQLQEELEGL 643
Cdd:COG4913    419 RELRELEAEIASL 431
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
569-646 1.81e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQL------------ALQKKEEVEAQVKQL 636
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreLEEELEELEAELAEL 175

                          90
                  ....*....|....
gi 1722504626 637 QEE----LEGLGVA 646
Cdd:COG4717   176 QEEleelLEQLSLA 189
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
 689-728 1.92e-03

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: 36.47  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1722504626 689 AKQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKG 728
Cdd:cd16510     1 EKLCKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 569-643 2.58e-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: 2.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626  569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 643
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 569-643 2.67e-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: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELEGL 643
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 569-641 2.70e-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: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVKQLQEELE 641
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 570-640 2.75e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 38.99  E-value: 2.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722504626 570 LARVRRQLDEAKRK---IRQweeswqqvkqvcDAWQREAQ---EAKERARvADSDRQLAlQKKEEVEAQVKQLQEEL 640
Cdd:PRK05759   58 QAKYEAQLAEARAEaaeIIE------------QAKKRAAQiieEAKAEAE-AEAARIKA-QAQAEIEQERKRAREEL 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 569-691 3.19e-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: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626  569 ELARVRRQLDEAKRKIRQWEESWQQVKQvcDAWQREAQEAKERARVadsdrQLALQKKEEVEAQVKQLQEELEGLGVAST 648
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRS--KVAQLELQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLKKLE 431

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1722504626  649 LPGLRGC-GDIGTIPlPKLHSLQSQLRLDLEAVDGVIFQLRAKQ 691
Cdd:TIGR02168  432 EAELKELqAELEELE-EELEELQEELERLEEALEELREELEEAE 474
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
569-643 3.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQV---CDAWQREAQEAKERARVADSDRQL--ALQKKEEVEAQVKQLQEELEGL 643
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEEL 151
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
 688-728 3.87e-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: 35.95  E-value: 3.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1722504626 688 RAKQCVACRERAHGAVLRPCQHHILCEPCA-----ATAPECPYCKG 728
Cdd:cd23128     2 RERECVMCMEEERSVVFLPCAHQVVCSGCNdlhekKGMRECPSCRG 47
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 690-727 4.29e-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: 4.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCAATA--PECPYCK 727
Cdd:cd16649     1 GLCVVCLENPASVLLLPCRHLCLCEVCAKGLrgKTCPICR 40
RING-HC_MEX3C cd16722
RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger ...
 692-732 4.34e-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: 36.11  E-value: 4.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1722504626 692 CVACRERAHGAVLRPCQHHILCEPCA-----ATAPECPYCKG---QPLQ 732
Cdd:cd16722     4 CVICFENEVIAALVPCGHNLFCMECAnkiceKETPSCPVCQTavtQAIQ 52
RING-HC_MEX3A cd16720
RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger ...
 689-726 5.44e-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: 35.70  E-value: 5.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1722504626 689 AKQCVACRERAHGAVLRPCQHHILCEPCAA-----TAPECPYC 726
Cdd:cd16720     2 GRDCMVCFESEVTAALVPCGHNLFCMECAVricerNEPECPVC 44
RING-HC_MEX3 cd16518
RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 ...
 690-732 6.72e-03

RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 family; MEX-3 phosphoproteins are found in vertebrates. They are mediators of post-transcriptional regulation in different organisms, and have been implicated in many core biological processes, including embryonic development, epithelial homeostasis, immune responses, metabolism, and cancer. They contain two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. They shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The RNA-binding protein MEX-3 from nematode Caenorhabditis elegans is the founding member of the MEX-3 family. Due to the lack of a RING-HC finger, it is not included here.


Pssm-ID: 438181 [Multi-domain]  Cd Length: 53  Bit Score: 35.42  E-value: 6.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1722504626 690 KQCVACRERAHGAVLRPCQHHILCEPCA-----ATAPECPYCKGQPLQ 732
Cdd:cd16518     1 RDCVVCFESEVVAALVPCGHNLFCMECAnriceKSDPECPVCHTPVTQ 48
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 569-643 6.99e-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: 6.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQV---KQVcDAWQREAQEAKERARVADsDRQLALQKK-EEVEAQVKQLQEELEGL 643
Cdd:COG1579    60 EIKRLELEIEEVEARIKKYEEQLGNVrnnKEY-EALQKEIESLKRRISDLE-DEILELMERiEELEEELAELEAELAEL 136
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
 689-726 7.00e-03

RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger and KH domain-containing protein 3 (RKHD3), or RING finger protein 195 (RNF195), 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 regulates the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions. It has a 3' long conserved untranslated region (3'LCU)-mediated fine-tuning system for mRNA regulation in early vertebrate development such as anteroposterior (AP) patterning and signal transduction. MEX3B 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, MEX3B shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438381 [Multi-domain]  Cd Length: 58  Bit Score: 35.43  E-value: 7.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1722504626 689 AKQCVACRERAHGAVLRPCQHHILCEPCA-----ATAPECPYC 726
Cdd:cd16721     4 SRDCSICFESEVIAALVPCGHNLFCMECAnriceKNEPQCPVC 46
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
 688-726 8.20e-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: 35.50  E-value: 8.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1722504626 688 RAKQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYC 726
Cdd:cd16714    13 EEKLCKICMDRNISIVFIPCGHLVTCKQCAEALDKCPIC 51
fliH PRK06669
flagellar assembly protein H; Validated
 569-641 8.21e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 38.84  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626 569 ELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSD---------RQLALQKKEEVEAQVKQLQEE 639
Cdd:PRK06669   21 EIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEiveaaeeeaKEELLKKTDEASSIIEKLQMQ 100


                  ..
gi 1722504626 640 LE 641
Cdd:PRK06669  101 IE 102
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
569-643 9.01e-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: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722504626  569 ELARVRRQLDEAKRKIRQW--EESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQ--------VKQLQE 638
Cdd:COG4913    266 AARERLAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLER 345


                   ....*
gi 1722504626  639 ELEGL 643
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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