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Conserved domains on  [gi|1276317456|ref|NP_001344805|]
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putative E3 ubiquitin-protein ligase UNKL isoform 4 [Mus musculus]

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 ...
 608-651 9.89e-18

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: 77.14  E-value: 9.89e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKGQPLPW 651
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 2.58e-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.


The actual alignment was detected with superfamily member pfam18384:

Pssm-ID: 375810  Cd Length: 40  Bit Score: 67.18  E-value: 2.58e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1276317456  25 YRYLKEFRTEQCSLFLQHKCSQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-560 1.45e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSD-------RQLALQRKEEVEAKVKQLQEELE 560
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-310 6.30e-04

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


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 37.56  E-value: 6.30e-04
                          10        20
                  ....*....|....*....|....*
gi 1276317456 286 YKSTKCNDMRQTGYCPRGPFCAFAH 310
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAH 25
 
Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 608-651 9.89e-18

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: 77.14  E-value: 9.89e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKGQPLPW 651
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 2.58e-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: 67.18  E-value: 2.58e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1276317456  25 YRYLKEFRTEQCSLFLQHKCSQHRPFTCFHWHFLNQ 60
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
608-645 6.44e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 43.52  E-value: 6.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCA----ASTPECPYCK 645
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAerllRKKKKCPICR 44
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-560 1.45e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSD-------RQLALQRKEEVEAKVKQLQEELE 560
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 488-609 1.72e-04

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: 43.51  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERArvadsDRQLA---LQRKEEVEAKVKQLQEELEglgl 564
Cdd:pfam04012  37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG-----NEELAreaLAEKKSLEKQAEALETQLA---- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1276317456 565 sslpglqslgdisdiplpKLHSLQSKLRLDLEAVDGVIFQLRAKQ 609
Cdd:pfam04012 108 ------------------QQRSAVEQLRKQLAALETKIQQLKAKK 134
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-310 6.30e-04

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 37.56  E-value: 6.30e-04
                          10        20
                  ....*....|....*....|....*
gi 1276317456 286 YKSTKCNDMRQTGYCPRGPFCAFAH 310
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAH 25
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 488-563 1.15e-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: 42.35  E-value: 1.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDawQREAQEAKERARVadsdrQLALQRKEEVEAKVKQLQEELEGLG 563
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELL 427
 
Name Accession Description Interval E-value
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 608-651 9.89e-18

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: 77.14  E-value: 9.89e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKGQPLPW 651
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 2.58e-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: 67.18  E-value: 2.58e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1276317456  25 YRYLKEFRTEQCSLFLQHKCSQHRPFTCFHWHFLNQ 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 ...
 608-645 4.46e-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: 63.73  E-value: 4.46e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCK 645
Cdd:cd16614     1 KKCMKCEERNRSVAVLPCQHYVLCEQCAETATECPYCH 38
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
608-645 6.44e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 43.52  E-value: 6.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCA----ASTPECPYCK 645
Cdd:pfam13920   3 LLCVICLDRPRNVVLLPCGHLCLCEECAerllRKKKKCPICR 44
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-560 1.45e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSD-------RQLALQRKEEVEAKVKQLQEELE 560
Cdd:COG4372    67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleelqkeRQDLEQQRKQLEAQIAELQSEIA 146
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
488-562 1.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEE---SWQQVKQACDAWQREAQEAKERARVADSDR-QLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG4717   140 ELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEA 218
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
488-562 2.59e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 45.97  E-value: 2.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARvaDSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG1842    38 DLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGR--EDLAREALERKAELEAQAEALEAQLAQL 110
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
 610-644 3.26e-05

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: 41.35  E-value: 3.26e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1276317456 610 CVACQERahGTVLRPCQHRVLCEPCAASTpECPYC 644
Cdd:cd16771     5 CLKCQEL--KRVTLPCQHALLCETCATSE-ECPIC 36
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 488-562 3.27e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 3.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG1196   359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
488-560 6.11e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 6.11e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSD-RQLALQRKEEVEAKVKQLQEELE 560
Cdd:COG4913    282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELE 355
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-562 6.47e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 6.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
489-631 1.03e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456  489 LARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLAlqrkeEVEAKVKQLQEELEGLGLSSlP 568
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASS-D 685

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276317456  569 GLQSLGDISDiplpKLHSLQSKLRLDLEAVDGVIFQLRAK------QCVACQERAHGTVLRPCQHRVLC 631
Cdd:COG4913    686 DLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKEleqaeeELDELQDRLEAAEDLARLELRAL 750
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
 607-646 1.03e-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: 39.93  E-value: 1.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1276317456 607 AKQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKG 646
Cdd:cd16510     1 EKLCKICMDREVNIVFLPCGHLVTCAQCAASLRKCPICRT 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-563 1.16e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGLG 563
Cdd:COG4372    95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 488-609 1.72e-04

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: 43.51  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERArvadsDRQLA---LQRKEEVEAKVKQLQEELEglgl 564
Cdd:pfam04012  37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG-----NEELAreaLAEKKSLEKQAEALETQLA---- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1276317456 565 sslpglqslgdisdiplpKLHSLQSKLRLDLEAVDGVIFQLRAKQ 609
Cdd:pfam04012 108 ------------------QQRSAVEQLRKQLAALETKIQQLKAKK 134
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
488-573 1.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQL------------ALQRKEEVEAKVKQL 555
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreLEEELEELEAELAEL 175

                          90       100
                  ....*....|....*....|..
gi 1276317456 556 QEEL----EGLGLSSLPGLQSL 573
Cdd:COG4717   176 QEELeellEQLSLATEEELQDL 197
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-562 1.90e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIrqwEESWQQVKQAcdawQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG4372    60 ELEQLEEELEQARSEL---EQLEEELEEL----NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-562 2.46e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEA-KERARVADSDRQLALQRKE------EVEAKVKQLQEELE 560
Cdd:COG4372    81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqKERQDLEQQRKQLEAQIAElqseiaEREEELKELEEQLE 160


                  ..
gi 1276317456 561 GL 562
Cdd:COG4372   161 SL 162
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 488-560 2.57e-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: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEA---------------KERARVADSDR---QLALQRKEEVE 549
Cdd:pfam20492  21 ETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAeeekerleesaemeaEEKEQLEAELAeaqEEIARLEEEVE 100

                          90
                  ....*....|....
gi 1276317456 550 AK---VKQLQEELE 560
Cdd:pfam20492 101 RKeeeARRLQEELE 114
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
488-562 2.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.63e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADS---DRQLALQRKEEVEAKV-KQLQEELEGL 562
Cdd:COG4913    700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVERELrENLEERIDAL 778
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
488-562 4.02e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456  488 ELARVRRQLDEAKRKIRQ----------WEESWQQ------VKQACDAW--QREAQEAKERARVADSDRQLALQRKEEVE 549
Cdd:COG4913    236 DLERAHEALEDAREQIELlepirelaerYAAARERlaeleyLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLE 315

                           90
                   ....*....|...
gi 1276317456  550 AKVKQLQEELEGL 562
Cdd:COG4913    316 ARLDALREELDEL 328
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
 610-647 4.12e-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: 38.43  E-value: 4.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1276317456 610 CVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKGQ 647
Cdd:cd16515     4 CVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRAD 41
DUF2058 pfam09831
Uncharacterized protein conserved in bacteria (DUF2058); This domain, found in various ...
 497-558 4.52e-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: 41.41  E-value: 4.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276317456 497 DEAK-RKIRQweESWQQVKQACDAWQ-REAQEAKERARV--ADSDRQLALQRKEEVEAK-----VKQLQEE 558
Cdd:pfam09831  13 DKKKaKQAKK--EKRKQRKQKRKKGAvDEAKAAAEEAKAekAERDRELNRQRQAEAEQKalaaqIRQLIEQ 81
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
286-310 6.30e-04

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 37.56  E-value: 6.30e-04
                          10        20
                  ....*....|....*....|....*
gi 1276317456 286 YKSTKCNDMRQTGYCPRGPFCAFAH 310
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAH 25
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
488-562 6.77e-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: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQAC-----------DAWQREAQEAKERARVADSDRQL-------ALQRKEEVE 549
Cdd:COG4913    339 RLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEAleealaeAEAALRDLR 418

                           90
                   ....*....|...
gi 1276317456  550 AKVKQLQEELEGL 562
Cdd:COG4913    419 RELRELEAEIASL 431
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-562 6.96e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG4372    46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 488-562 8.24e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
 608-645 9.45e-04

Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING finger domain protein 1 (CGRRF1) and similar proteins; 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. CGRRF1 contains a C-terminal 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.


Pssm-ID: 438441 [Multi-domain]  Cd Length: 38  Bit Score: 37.35  E-value: 9.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCK 645
Cdd:cd16787     1 KDCVVCQNAPVNRVLLPCRHACVCDECFKRLQRCPMCR 38
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 488-560 1.14e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQ---QVKQACDAWQREAQEAKERARVadsDRQLALQRKEEVEAKVKQLQEELE 560
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAklyQEEQERKERQKEREEAEKKARQ---RQELQQAREEQIELKERRLAEEAE 257
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 488-563 1.15e-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: 42.35  E-value: 1.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDawQREAQEAKERARVadsdrQLALQRKEEVEAKVKQLQEELEGLG 563
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELL 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 488-562 1.23e-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: 41.97  E-value: 1.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
 606-645 1.33e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 36.95  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1276317456 606 RAKQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCK 645
Cdd:cd16566     1 REDSCTLCFDKVADTELRPCGHSGFCMECALQLETCPLCR 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 488-560 1.70e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELE 560
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
488-560 1.77e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276317456 488 ELARVRRQLDEAKRKIRqwEESWQQVKQAcdawQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELE 560
Cdd:COG4717   171 ELAELQEELEELLEQLS--LATEEELQDL----AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 608-645 1.80e-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: 36.53  E-value: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAAS--TPECPYCK 645
Cdd:cd16649     1 GLCVVCLENPASVLLLPCRHLCLCEVCAKGlrGKTCPICR 40
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
491-560 1.95e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 1.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317456 491 RVRRQLDEAKRKIRQWEEswqQVKQACDAWQ----REAQEAKERA--RVADSDRQLALQRKEEVEAK--VKQLQEELE 560
Cdd:COG1842    55 RLERQLEELEAEAEKWEE---KARLALEKGRedlaREALERKAELeaQAEALEAQLAQLEEQVEKLKeaLRQLESKLE 129
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 488-609 2.01e-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: 41.58  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456  488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERAR-------VADSDRQLALQRKEEVEAKVKQLQEELE 560
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleELEAQLEELESKLDELAEELAELEEKLE 347

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1276317456  561 GLgLSSLPGLQSLGDISDIPLPKLHSLQSKLRLDLEAVDGVIFQLRAKQ 609
Cdd:TIGR02168  348 EL-KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
 606-646 2.03e-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: 36.72  E-value: 2.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1276317456 606 RAKQCVACQERAHGTVLRPCQHRVLCEPCA-----ASTPECPYCKG 646
Cdd:cd23128     2 RERECVMCMEEERSVVFLPCAHQVVCSGCNdlhekKGMRECPSCRG 47
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
 608-646 2.75e-03

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other IAPs, such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs 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), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), kidney inhibitor of apoptosis protein (KIAP), melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 438373 [Multi-domain]  Cd Length: 57  Bit Score: 36.30  E-value: 2.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCKG 646
Cdd:cd16713     8 RTCKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRA 46
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 489-560 2.78e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.87  E-value: 2.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276317456 489 LARVRRQLDEAKRkiRQWEESWQQVKQacdawQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELE 560
Cdd:pfam05672  22 QAREQREREEQER--LEKEEEERLRKE-----ELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE 86
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 488-562 3.19e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.93  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKER----ARVADSDRQLALQR-------KEEVEAKVKQLQ 556
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkfLKENDAKRRRALKKaeeetklKKEKEKEIKKLT 86


                  ....*.
gi 1276317456 557 EELEGL 562
Cdd:pfam13863  87 AQIEEL 92
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
 606-644 3.36e-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: 36.27  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1276317456 606 RAKQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYC 644
Cdd:cd16714    13 EEKLCKICMDRNISIVFIPCGHLVTCKQCAEALDKCPIC 51
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 494-558 4.09e-03

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: 37.59  E-value: 4.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 494 RQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEE 558
Cdd:pfam20492   6 REKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
 608-645 4.53e-03

RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1.


Pssm-ID: 438182  Cd Length: 38  Bit Score: 35.15  E-value: 4.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1276317456 608 KQCVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCK 645
Cdd:cd16519     1 EECRVCSDKKALVLFQPCGHVVACEECSLRMKKCLQCK 38
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
488-562 5.03e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESwQQVKQACDAWQREAQEAKERARvADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELR-EELEKLEKLLQLLPLYQELEALEAELAEL 144
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 488-562 6.59e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRKEEVEAKVKQLQEELEGL 562
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
 610-645 6.93e-03

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARP subfamily includes CARP-1 and CARP-2 proteins, both of which are E3 ubiquitin ligases that ubiquitinate apical caspases and target them for proteasome-mediated degradation. As a novel group of caspase regulators with a FYVE-type zinc finger domain, they do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8, and caspase 10. Moreover, they stabilize MDM2 by inhibiting MDM2 self-ubiquitination, as well as by targeting 14-3-3sigma for degradation. They work together with MDM2 to enhance p53 degradation, thereby inhibiting p53-mediated cell death. CARPs contain an N-terminal FYVE-like domain that can serve as a membrane-targeting or endosome localizing signal and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 438163 [Multi-domain]  Cd Length: 48  Bit Score: 35.05  E-value: 6.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1276317456 610 CVACQERAHGTVLRPCQHRVLCEPCAASTPECPYCK 645
Cdd:cd16500     3 CKICMDAAIDCVLLECGHMVTCTDCGKKLSECPICR 38
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 488-563 9.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317456 488 ELARVRRQLDEAKRKIRQWEESWQQVKQACDAWQREAQEAKERARVADSDRQLALQRK---------------------E 546
Cdd:COG1196   684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELleeeelleeealeelpeppdlE 763

                          90
                  ....*....|....*..
gi 1276317456 547 EVEAKVKQLQEELEGLG 563
Cdd:COG1196   764 ELERELERLEREIEALG 780
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
 606-645 9.84e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 34.93  E-value: 9.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1276317456 606 RAKQCVACQERAHGTVLRPCQHRVLCEPCA----ASTPECPYCK 645
Cdd:cd23129     1 QRDECVVCMDAPRDAVCVPCGHVAGCMSCLkalmQSSPLCPICR 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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