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Conserved domains on  [gi|9755831|emb|CAC01862|]
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putative protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cast super family cl37807
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 71-334 3.35e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


The actual alignment was detected with superfamily member pfam10174:

Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 51.36  E-value: 3.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831      71 QSLLEEKEAlaeKLAISEYEFRLAQEDIARLKTEGQkksVPSIDKSEEMdsdefggNRPEIQRKKKDFSFTDIGPLKnne 150
Cdd:pfam10174  232 QTVIEMKDT---KISSLERNIRDLEDEVQMLKTNGL---LHTEDREEEI-------KQMEVYKSHSKFMKNKIDQLK--- 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     151 rQDLNcaVKEYLLLAgyrltAMTFYEEVTDQNLDVWQdspaHVpdalryyyyQYLSSTSEAAEEKIAMLQ---------- 220
Cdd:pfam10174  296 -QELS--KKESELLA-----LQTKLETLTNQNSDCKQ----HI---------EVLKESLTAKEQRAAILQtevdalrlrl 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     221 -ENESL----KKEIERLSKEKDGLLKSKENF-------EEQIGAFNKSTESLQKDLRDREKQVQSLK---QSSEHQRRN- 284
Cdd:pfam10174  355 eEKESFlnkkTKQLQDLTEEKSTLAGEIRDLkdmldvkERKINVLQKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNt 434

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     285 ------LNDCRAE----ITSLKMHIEGSRAgqyVSLNEGDPVKLQSKEVEEQISTLSEEV 334
Cdd:pfam10174  435 dtalttLEEALSEkeriIERLKEQREREDR---ERLEELESLKKENKDLKEKVSALQPEL 491
UBCc_UEV super family cl49610
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 1059-1088 5.70e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin, and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways.


The actual alignment was detected with superfamily member cd23798:

Pssm-ID: 483950 [Multi-domain]  Cd Length: 152  Bit Score: 38.67  E-value: 5.70e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 9755831  1059 SQTSVKEYLLpAIQNLLKDPDALDPAHKEA 1088
Cdd:cd23798  102 PSITIKQILL-GIQDLLDEPNLDDPAQAEA 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-472 8.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   209 SEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDC 288
Cdd:COG4372   55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   289 RAEITSLKMHIEgSRAGQYVSLNEgdpvklQSKEVEEQISTLSEEVVN-PTVEKDGGLISKVSISAEKGHIQTEDDMVVE 367
Cdd:COG4372  135 EAQIAELQSEIA-EREEELKELEE------QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   368 EVKNIIADQREVAGEAGNISYANNGTLENQKEVSNYLLSPSNGNFSPRDLGSILKVDPGIGRDSNSKSDNANGEAASEEM 447
Cdd:COG4372  208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287

                        250       260
                 ....*....|....*....|....*
gi 9755831   448 ASTSFDIVNGLGTIQILADALPNIV 472
Cdd:COG4372  288 LEEAALELKLLALLLNLAALSLIGA 312
 
Name Accession Description Interval E-value
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 71-334 3.35e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 51.36  E-value: 3.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831      71 QSLLEEKEAlaeKLAISEYEFRLAQEDIARLKTEGQkksVPSIDKSEEMdsdefggNRPEIQRKKKDFSFTDIGPLKnne 150
Cdd:pfam10174  232 QTVIEMKDT---KISSLERNIRDLEDEVQMLKTNGL---LHTEDREEEI-------KQMEVYKSHSKFMKNKIDQLK--- 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     151 rQDLNcaVKEYLLLAgyrltAMTFYEEVTDQNLDVWQdspaHVpdalryyyyQYLSSTSEAAEEKIAMLQ---------- 220
Cdd:pfam10174  296 -QELS--KKESELLA-----LQTKLETLTNQNSDCKQ----HI---------EVLKESLTAKEQRAAILQtevdalrlrl 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     221 -ENESL----KKEIERLSKEKDGLLKSKENF-------EEQIGAFNKSTESLQKDLRDREKQVQSLK---QSSEHQRRN- 284
Cdd:pfam10174  355 eEKESFlnkkTKQLQDLTEEKSTLAGEIRDLkdmldvkERKINVLQKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNt 434

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     285 ------LNDCRAE----ITSLKMHIEGSRAgqyVSLNEGDPVKLQSKEVEEQISTLSEEV 334
Cdd:pfam10174  435 dtalttLEEALSEkeriIERLKEQREREDR---ERLEELESLKKENKDLKEKVSALQPEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 205-326 5.44e-06

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: 50.83  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     205 LSSTSEAAEEKIAMLQEN-ESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRR 283
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 9755831     284 NLNDCRAEITSLKM---HIEGSRAGQYvSLNEGDPVKLQSKEVEEQ 326
Cdd:TIGR02168  923 KLAQLELRLEGLEVridNLQERLSEEY-SLTLEEAEALENKIEDDE 967
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 206-292 1.81e-04

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: 45.14  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   206 SSTSEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNL 285
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99


                 ....*..
gi 9755831   286 NDCRAEI 292
Cdd:COG4942  100 EAQKEEL 106
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
205-332 7.46e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831    205 LSSTSEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLK--QSSEHQR 282
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEY 295

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 9755831    283 RNLNDCRAEITSLKMHIEgSRAGQYVSlnegdpvklQSKEVEEQISTLSE 332
Cdd:PRK03918  296 IKLSEFYEEYLDELREIE-KRLSRLEE---------EINGIEERIKELEE 335
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 200-296 8.56e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.74  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   200 YYYQYLSSTSEAAEEKIAMLQEN--ESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSL--K 275
Cdd:cd22656   92 YYAEILELIDDLADATDDEELEEakKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltD 171

                         90       100
                 ....*....|....*....|.
gi 9755831   276 QSSEHQRRNLNDCRAEITSLK 296
Cdd:cd22656  172 EGGAIARKEIKDLQKELEKLN 192
UBCc_UBE2I cd23798
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I ...
 1059-1088 5.70e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I and related proteins; The E2I subfamily includes mammalian ubiquitin-conjugating enzymes E2 I (UBE2I/UBC9/UBCE9, EC 2.3.2.-), yeast ubiquitin-conjugating enzyme E2-18 kDa (UBC9, EC2.3.2.-), and plant SUMO-conjugating enzyme 1 (SCE1/AHUS5, EC2.3.2.-). UBE2I, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, SUMO-protein ligase, ubiquitin carrier protein 9, ubiquitin carrier protein I, or ubiquitin-protein ligase I, accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. It can catalyze the formation of poly-SUMO chains. It is necessary for sumoylation of FOXL2 and KAT5 and essential for nuclear architecture and chromosome segregation. UBE2I also sumoylates p53/TP53 at 'Lys-386' and mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity. Saccharomyces cerevisiae UBC9, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, ubiquitin carrier protein 9, ubiquitin-conjugating enzyme E2-18 kDa, acts as an E2 ubiquitin-like--protein ligase that mediates SUMO/Smt3 attachment to septins and PCNA. It may be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2). Arabidopsis thaliana SCE1, also called SUMO-conjugating enzyme SCE1, protein EMBRYO DEFECTIVE 1637, or protein hus5 homolog, is a SUMO-conjugating enzyme that accepts the SUMO proteins from the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21. It associates with SIZ1 for sumoylation of the transcription factor GTE3.


Pssm-ID: 467418 [Multi-domain]  Cd Length: 152  Bit Score: 38.67  E-value: 5.70e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 9755831  1059 SQTSVKEYLLpAIQNLLKDPDALDPAHKEA 1088
Cdd:cd23798  102 PSITIKQILL-GIQDLLDEPNLDDPAQAEA 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-472 8.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   209 SEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDC 288
Cdd:COG4372   55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   289 RAEITSLKMHIEgSRAGQYVSLNEgdpvklQSKEVEEQISTLSEEVVN-PTVEKDGGLISKVSISAEKGHIQTEDDMVVE 367
Cdd:COG4372  135 EAQIAELQSEIA-EREEELKELEE------QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   368 EVKNIIADQREVAGEAGNISYANNGTLENQKEVSNYLLSPSNGNFSPRDLGSILKVDPGIGRDSNSKSDNANGEAASEEM 447
Cdd:COG4372  208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287

                        250       260
                 ....*....|....*....|....*
gi 9755831   448 ASTSFDIVNGLGTIQILADALPNIV 472
Cdd:COG4372  288 LEEAALELKLLALLLNLAALSLIGA 312
 
Name Accession Description Interval E-value
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 71-334 3.35e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 51.36  E-value: 3.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831      71 QSLLEEKEAlaeKLAISEYEFRLAQEDIARLKTEGQkksVPSIDKSEEMdsdefggNRPEIQRKKKDFSFTDIGPLKnne 150
Cdd:pfam10174  232 QTVIEMKDT---KISSLERNIRDLEDEVQMLKTNGL---LHTEDREEEI-------KQMEVYKSHSKFMKNKIDQLK--- 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     151 rQDLNcaVKEYLLLAgyrltAMTFYEEVTDQNLDVWQdspaHVpdalryyyyQYLSSTSEAAEEKIAMLQ---------- 220
Cdd:pfam10174  296 -QELS--KKESELLA-----LQTKLETLTNQNSDCKQ----HI---------EVLKESLTAKEQRAAILQtevdalrlrl 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     221 -ENESL----KKEIERLSKEKDGLLKSKENF-------EEQIGAFNKSTESLQKDLRDREKQVQSLK---QSSEHQRRN- 284
Cdd:pfam10174  355 eEKESFlnkkTKQLQDLTEEKSTLAGEIRDLkdmldvkERKINVLQKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNt 434

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     285 ------LNDCRAE----ITSLKMHIEGSRAgqyVSLNEGDPVKLQSKEVEEQISTLSEEV 334
Cdd:pfam10174  435 dtalttLEEALSEkeriIERLKEQREREDR---ERLEELESLKKENKDLKEKVSALQPEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 205-326 5.44e-06

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: 50.83  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     205 LSSTSEAAEEKIAMLQEN-ESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRR 283
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 9755831     284 NLNDCRAEITSLKM---HIEGSRAGQYvSLNEGDPVKLQSKEVEEQ 326
Cdd:TIGR02168  923 KLAQLELRLEGLEVridNLQERLSEEY-SLTLEEAEALENKIEDDE 967
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-333 5.12e-05

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: 47.74  E-value: 5.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     203 QYLSSTSEAAEEKIAML-QENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQ 281
Cdd:TIGR02168  312 ANLERQLEELEAQLEELeSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 9755831     282 RRNLNDCRAEITSLKMHIEGS-----RAGQYVSLNEGDPVKLQSKEVEEQISTLSEE 333
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLedrreRLQQEIEELLKKLEEAELKELQAELEELEEE 448
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 206-292 1.81e-04

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: 45.14  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   206 SSTSEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNL 285
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99


                 ....*..
gi 9755831   286 NDCRAEI 292
Cdd:COG4942  100 EAQKEEL 106
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 220-334 2.52e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     220 QENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDCRAEITSLKMHI 299
Cdd:TIGR04523  405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 9755831     300 EGSRAGQYVSLNEGDPVKLQSKEVEEQISTLSEEV 334
Cdd:TIGR04523  485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
205-332 7.46e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831    205 LSSTSEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLK--QSSEHQR 282
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEY 295

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 9755831    283 RNLNDCRAEITSLKMHIEgSRAGQYVSlnegdpvklQSKEVEEQISTLSE 332
Cdd:PRK03918  296 IKLSEFYEEYLDELREIE-KRLSRLEE---------EINGIEERIKELEE 335
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 200-296 8.56e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.74  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   200 YYYQYLSSTSEAAEEKIAMLQEN--ESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSL--K 275
Cdd:cd22656   92 YYAEILELIDDLADATDDEELEEakKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltD 171

                         90       100
                 ....*....|....*....|.
gi 9755831   276 QSSEHQRRNLNDCRAEITSLK 296
Cdd:cd22656  172 EGGAIARKEIKDLQKELEKLN 192
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-334 1.35e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   209 SEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDC 288
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 9755831   289 RAEITSLKMHIEgSRAGQYVSLNEgdpvklQSKEVEEQISTLSEEV 334
Cdd:COG4372  107 QEEAEELQEELE-ELQKERQDLEQ------QRKQLEAQIAELQSEI 145
PRK12704 PRK12704
phosphodiesterase; Provisional
 199-333 1.46e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831    199 YYYYQYLSSTSEAAEEKIA--MLQ----ENESLKKEIERLSKEKdgLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQ 272
Cdd:PRK12704   22 YFVRKKIAEAKIKEAEEEAkrILEeakkEAEAIKKEALLEAKEE--IHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9755831    273 SLKQSSEHQRRNLNDCRAEITSLKMHIEGSRAgqyvSLNEgdpvkLQSKEVE--EQISTLSEE 333
Cdd:PRK12704  100 RKLELLEKREEELEKKEKELEQKQQELEKKEE----ELEE-----LIEEQLQelERISGLTAE 153
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
210-402 1.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   210 EAAEEKIAMLQ-ENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQ---SSEHQRRNL 285
Cdd:COG4372   97 AQAQEELESLQeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaALEQELQAL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   286 NDCRAEiTSLKMHIEGSRAGQYVSLNEGDPVKLQSKEVEEQISTLSEEVVNPTVEKDGGLISKVSISAEKGHIQTEDDMV 365
Cdd:COG4372  177 SEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 9755831   366 VEEVKNIIADQREVAGEAGNISYANNGTLENQKEVSN 402
Cdd:COG4372  256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 189-301 4.44e-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: 40.90  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   189 SPAHVPDALR-YYYYQYLSStseaaeekiAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDR 267
Cdd:COG4942  127 SPEDFLDAVRrLQYLKYLAP---------ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 9755831   268 EKQVQSLKQSSEHQRRNLNDCRAEITSLKMHIEG 301
Cdd:COG4942  198 QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
 223-276 5.63e-03

C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 36.57  E-value: 5.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 9755831   223 ESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQ 276
Cdd:cd22301    5 KNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRK 58
UBCc_UBE2I cd23798
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I ...
 1059-1088 5.70e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I and related proteins; The E2I subfamily includes mammalian ubiquitin-conjugating enzymes E2 I (UBE2I/UBC9/UBCE9, EC 2.3.2.-), yeast ubiquitin-conjugating enzyme E2-18 kDa (UBC9, EC2.3.2.-), and plant SUMO-conjugating enzyme 1 (SCE1/AHUS5, EC2.3.2.-). UBE2I, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, SUMO-protein ligase, ubiquitin carrier protein 9, ubiquitin carrier protein I, or ubiquitin-protein ligase I, accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. It can catalyze the formation of poly-SUMO chains. It is necessary for sumoylation of FOXL2 and KAT5 and essential for nuclear architecture and chromosome segregation. UBE2I also sumoylates p53/TP53 at 'Lys-386' and mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity. Saccharomyces cerevisiae UBC9, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, ubiquitin carrier protein 9, ubiquitin-conjugating enzyme E2-18 kDa, acts as an E2 ubiquitin-like--protein ligase that mediates SUMO/Smt3 attachment to septins and PCNA. It may be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2). Arabidopsis thaliana SCE1, also called SUMO-conjugating enzyme SCE1, protein EMBRYO DEFECTIVE 1637, or protein hus5 homolog, is a SUMO-conjugating enzyme that accepts the SUMO proteins from the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21. It associates with SIZ1 for sumoylation of the transcription factor GTE3.


Pssm-ID: 467418 [Multi-domain]  Cd Length: 152  Bit Score: 38.67  E-value: 5.70e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 9755831  1059 SQTSVKEYLLpAIQNLLKDPDALDPAHKEA 1088
Cdd:cd23798  102 PSITIKQILL-GIQDLLDEPNLDDPAQAEA 130
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 221-300 6.27e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 6.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831     221 ENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDCRAEITSLKMHIE 300
Cdd:TIGR04523  378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-472 8.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   209 SEAAEEKIAMLQENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDC 288
Cdd:COG4372   55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   289 RAEITSLKMHIEgSRAGQYVSLNEgdpvklQSKEVEEQISTLSEEVVN-PTVEKDGGLISKVSISAEKGHIQTEDDMVVE 367
Cdd:COG4372  135 EAQIAELQSEIA-EREEELKELEE------QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831   368 EVKNIIADQREVAGEAGNISYANNGTLENQKEVSNYLLSPSNGNFSPRDLGSILKVDPGIGRDSNSKSDNANGEAASEEM 447
Cdd:COG4372  208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287

                        250       260
                 ....*....|....*....|....*
gi 9755831   448 ASTSFDIVNGLGTIQILADALPNIV 472
Cdd:COG4372  288 LEEAALELKLLALLLNLAALSLIGA 312
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
221-379 9.99e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755831    221 ENESLKKEIERLSKEKDGLLKSKENFEEQIGAFNKSTESLQKDLRDREKQVQSLKQSSEHQRRNLNDCRAEITSLKMHIE 300
Cdd:PRK02224  308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9755831    301 gsragqyvslnegdpvklqskEVEEQISTLSEEVVNPTVEKDGgliskvsISAEKGHIQTEDDMVVEEVKNIIADQREV 379
Cdd:PRK02224  388 ---------------------ELEEEIEELRERFGDAPVDLGN-------AEDFLEELREERDELREREAELEATLRTA 438
 
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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