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Conserved domains on  [gi|578804055|ref|XP_006712477|]
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TRAF3-interacting protein 1 isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
465-618 2.93e-70

Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


:

Pssm-ID: 465481 [Multi-domain]  Cd Length: 154  Bit Score: 224.25  E-value: 2.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  465 EEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDV 544
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDRSLQESSAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804055  545 DAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSI 618
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both ...
5-117 2.55e-63

Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


:

Pssm-ID: 463020  Cd Length: 113  Bit Score: 204.21  E-value: 2.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055    5 VVRRTQEALGKVIRRPPLTEKLLSKPPFRYLHDIITEVIRMTGFMKGLYTDAEMKSDNVKDKDAKISFLQKAIDVVVMVS 84
Cdd:pfam10243   1 FVEPTQELLGAVIQKPKLTEKLLSKPPFKYIHDIIMETIKATGFPKGLYTDDELDSNNVNDKDAKIAFLQKLIDLVEMGS 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578804055   85 GEPLLAKPARIVAGHEPERTNELLQIIGKCCLN 117
Cdd:pfam10243  81 GKPVAAKPAKIVAGLEPEKTNELLQMLGRCATS 113
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
132-300 3.95e-06

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 132 EKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKEELKEDRKPREKDKDKEkakeNGGNR 211
Cdd:PRK12678 146 GEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE----ERGRR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 212 HREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEggkekerlrdrdrerdrdKGKDRDRRRVKNGEHSWDL 291
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR------------------RFRDRDRRGRRGGDGGNER 283

                 ....*....
gi 578804055 292 DREkNREHD 300
Cdd:PRK12678 284 EPE-LREDD 291
 
Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
465-618 2.93e-70

Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 465481 [Multi-domain]  Cd Length: 154  Bit Score: 224.25  E-value: 2.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  465 EEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDV 544
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDRSLQESSAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804055  545 DAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSI 618
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both ...
5-117 2.55e-63

Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 463020  Cd Length: 113  Bit Score: 204.21  E-value: 2.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055    5 VVRRTQEALGKVIRRPPLTEKLLSKPPFRYLHDIITEVIRMTGFMKGLYTDAEMKSDNVKDKDAKISFLQKAIDVVVMVS 84
Cdd:pfam10243   1 FVEPTQELLGAVIQKPKLTEKLLSKPPFKYIHDIIMETIKATGFPKGLYTDDELDSNNVNDKDAKIAFLQKLIDLVEMGS 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578804055   85 GEPLLAKPARIVAGHEPERTNELLQIIGKCCLN 117
Cdd:pfam10243  81 GKPVAAKPAKIVAGLEPEKTNELLQMLGRCATS 113
PRK12678 PRK12678
transcription termination factor Rho; Provisional
132-300 3.95e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 132 EKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKEELKEDRKPREKDKDKEkakeNGGNR 211
Cdd:PRK12678 146 GEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE----ERGRR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 212 HREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEggkekerlrdrdrerdrdKGKDRDRRRVKNGEHSWDL 291
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR------------------RFRDRDRRGRRGGDGGNER 283

                 ....*....
gi 578804055 292 DREkNREHD 300
Cdd:PRK12678 284 EPE-LREDD 291
PTZ00121 PTZ00121
MAEBL; Provisional
100-613 4.70e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  100 EPERTNELLQIIGKCCLNKLSSDDAVRRVLAGEKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTS 179
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  180 RDRKQKEELKEDRKPREKDKDKEKAKENGGNRHREGERERAKArARPDNERQKDRGNRERDRDSERKKETERKSEGGKEK 259
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  260 ERLRDRDRERDRDKGKDRDRRRVKNGEHSWDLDR--EKNREHDKPEKKSassgEMSKKLSDGTFKDSKAETETEISTRAS 337
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  338 KSLTTKTSKRRSKnsvegDSTSDAGDAGPAGQDKSEVPETPEIpnELSSNIRRIPRPGSARPAPPRVKRQDSMEALQMDR 417
Cdd:PTZ00121 1481 EAKKADEAKKKAE-----EAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  418 SGSGKTVSNVITESHNSDNEEDDQFVVEAAPQLSEMSEIEMVTAVELEEEEKHGGL--VKKILETKKDYEKLQQSpkpgE 495
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeAKKAEEAKIKAEELKKA----E 1629
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  496 KERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKimdyiQEDVDAMQNELQMWHSENRQHAEALQQEQRITDCA 575
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 578804055  576 VEPLKAELAEL---EQLIKDQQDKicAVKANILKNEEKIQK 613
Cdd:PTZ00121 1705 EELKKKEAEEKkkaEELKKAEEEN--KIKAEEAKKEAEEDK 1743
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
209-347 6.28e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 42.60  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  209 GNRHREGERERAKARARpDNERQKDRGnRERDRDSERKKETERKSEggkekerlrdRDRERDRDKGKDRDRRRVKNGEHS 288
Cdd:TIGR01622   1 RYRDRERERLRDSSSAG-DRDRRRDKG-RERSRDRSRDRERSRSRR----------RDRHRDRDYYRGRERRSRSRRPNR 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804055  289 WDLDREKNR---EHDKPEKKSASSGEMSKKLSDGTfKDSKAETETEISTRASKSLTTKTSKR 347
Cdd:TIGR01622  69 RYRPREKRRrrgDSYRRRRDDRRSRREKPRARDGT-PEPLTEDERDRRTVFVQQLAARARER 129
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
513-613 3.91e-03

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: 39.66  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 513 SKEIEKLRTSIQTLCKSalPLGKIMDYiQEDVDAMQNELQMWHSENRQHAEALQQ------------EQRITDCAVEPLK 580
Cdd:cd22656  109 DEELEEAKKTIKALLDD--LLKEAKKY-QDKAAKVVDKLTDFENQTEKDQTALETlekalkdlltdeGGAIARKEIKDLQ 185
                         90       100       110
                 ....*....|....*....|....*....|....
gi 578804055 581 AELAEL-EQLIKDQQDKICAVKANILKNEEKIQK 613
Cdd:cd22656  186 KELEKLnEEYAAKLKAKIDELKALIADDEAKLAA 219
 
Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
465-618 2.93e-70

Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 465481 [Multi-domain]  Cd Length: 154  Bit Score: 224.25  E-value: 2.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  465 EEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDV 544
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDRSLQESSAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804055  545 DAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSI 618
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both ...
5-117 2.55e-63

Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 463020  Cd Length: 113  Bit Score: 204.21  E-value: 2.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055    5 VVRRTQEALGKVIRRPPLTEKLLSKPPFRYLHDIITEVIRMTGFMKGLYTDAEMKSDNVKDKDAKISFLQKAIDVVVMVS 84
Cdd:pfam10243   1 FVEPTQELLGAVIQKPKLTEKLLSKPPFKYIHDIIMETIKATGFPKGLYTDDELDSNNVNDKDAKIAFLQKLIDLVEMGS 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578804055   85 GEPLLAKPARIVAGHEPERTNELLQIIGKCCLN 117
Cdd:pfam10243  81 GKPVAAKPAKIVAGLEPEKTNELLQMLGRCATS 113
PRK12678 PRK12678
transcription termination factor Rho; Provisional
132-300 3.95e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 132 EKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKEELKEDRKPREKDKDKEkakeNGGNR 211
Cdd:PRK12678 146 GEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE----ERGRR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 212 HREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEggkekerlrdrdrerdrdKGKDRDRRRVKNGEHSWDL 291
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR------------------RFRDRDRRGRRGGDGGNER 283

                 ....*....
gi 578804055 292 DREkNREHD 300
Cdd:PRK12678 284 EPE-LREDD 291
PTZ00121 PTZ00121
MAEBL; Provisional
100-613 4.70e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  100 EPERTNELLQIIGKCCLNKLSSDDAVRRVLAGEKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTS 179
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  180 RDRKQKEELKEDRKPREKDKDKEKAKENGGNRHREGERERAKArARPDNERQKDRGNRERDRDSERKKETERKSEGGKEK 259
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  260 ERLRDRDRERDRDKGKDRDRRRVKNGEHSWDLDR--EKNREHDKPEKKSassgEMSKKLSDGTFKDSKAETETEISTRAS 337
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  338 KSLTTKTSKRRSKnsvegDSTSDAGDAGPAGQDKSEVPETPEIpnELSSNIRRIPRPGSARPAPPRVKRQDSMEALQMDR 417
Cdd:PTZ00121 1481 EAKKADEAKKKAE-----EAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  418 SGSGKTVSNVITESHNSDNEEDDQFVVEAAPQLSEMSEIEMVTAVELEEEEKHGGL--VKKILETKKDYEKLQQSpkpgE 495
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeAKKAEEAKIKAEELKKA----E 1629
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  496 KERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKimdyiQEDVDAMQNELQMWHSENRQHAEALQQEQRITDCA 575
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 578804055  576 VEPLKAELAEL---EQLIKDQQDKicAVKANILKNEEKIQK 613
Cdd:PTZ00121 1705 EELKKKEAEEKkkaEELKKAEEEN--KIKAEEAKKEAEEDK 1743
PRK12678 PRK12678
transcription termination factor Rho; Provisional
120-301 1.11e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 48.36  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 120 SSDDAVRRVLAGEKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKEElKEDRKPREKDK 199
Cdd:PRK12678  89 QAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA-RADAAERTEEE 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 200 DKEKAKENGGNRHREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEGGKEKERLRDRDRERDRDKGKDRDR 279
Cdd:PRK12678 168 ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDR 247
                        170       180
                 ....*....|....*....|..
gi 578804055 280 RRVKNGEHSWDLDREKNREHDK 301
Cdd:PRK12678 248 GDRDGDDGEGRGGRRGRRFRDR 269
PRK12678 PRK12678
transcription termination factor Rho; Provisional
120-315 2.20e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.59  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 120 SSDDAVRRVLAGEKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKE-ELKEDRKPREKD 198
Cdd:PRK12678  69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEaARRGAARKAGEG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 199 KDKEKAKENGGNRHREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEGGKEKERLRDRDRERDRDKGKDRD 278
Cdd:PRK12678 149 GEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRG 228
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578804055 279 RRRVKNGEHSWDLDREKNREHDKPEKKSASSGEMSKK 315
Cdd:PRK12678 229 RRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRR 265
PRK12678 PRK12678
transcription termination factor Rho; Provisional
120-303 1.23e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 45.28  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 120 SSDDAVRRVLAGEKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKEELKEDRKPREKDK 199
Cdd:PRK12678  99 AAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDR 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 200 DKEKAKENGGNRHREGERERAKARARPDNERQkDRGNRERDRDSERKKETERKSEGGKEKERLRDRDRERDRDKGKDRDR 279
Cdd:PRK12678 179 EDRQAEAERGERGRREERGRDGDDRDRRDRRE-QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEG 257
                        170       180
                 ....*....|....*....|....
gi 578804055 280 RRVKNGEHSWDLDREKNREHDKPE 303
Cdd:PRK12678 258 RGGRRGRRFRDRDRRGRRGGDGGN 281
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
209-347 6.28e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 42.60  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  209 GNRHREGERERAKARARpDNERQKDRGnRERDRDSERKKETERKSEggkekerlrdRDRERDRDKGKDRDRRRVKNGEHS 288
Cdd:TIGR01622   1 RYRDRERERLRDSSSAG-DRDRRRDKG-RERSRDRSRDRERSRSRR----------RDRHRDRDYYRGRERRSRSRRPNR 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804055  289 WDLDREKNR---EHDKPEKKSASSGEMSKKLSDGTfKDSKAETETEISTRASKSLTTKTSKR 347
Cdd:TIGR01622  69 RYRPREKRRrrgDSYRRRRDDRRSRREKPRARDGT-PEPLTEDERDRRTVFVQQLAARARER 129
PTZ00121 PTZ00121
MAEBL; Provisional
125-610 3.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  125 VRRVLAGEKGEVKGRASLTSRSQELDN-------KNVREEESRVHKNTEDRGDAEIKERSTSR--------------DRK 183
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKaeavkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfarrqaaikaeEAR 1278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  184 QKEELKEDRKPREKDKDKEKAKEnggnRHREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEGGKEKERLR 263
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEK----KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  264 DRDRERDRDKGKDRDRRRVKNGEHSWDLDREKNREHDKPEKKSASSGEMSKKLSDGTFKDSKAETETEISTRASKSLTTK 343
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  344 TSKRRSKNSVEGDSTSDAGDAGPAGQDKSEVPETPEIPNELSSNIRRIPRPGSARPAPPRVKRQdsmeALQMDRSGSGKT 423
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKK 1510
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  424 VSNVITESHNSDNEEDDQFVVEA--APQLSEMSEIEMVTAVELEEEEKHGGLVKKILETKKDYEKLQQSPKPGEK----E 497
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaE 1590
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  498 RSLFESAWKKEKDIVSKEIEKLRTSIQTLCKsALPLGKimdyiQEDVDAMQNELQMWHSENRQHAEALQQEQRITDCAVE 577
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 578804055  578 PLKAELAE----LEQLIKDQQDKICAVKANILKNEEK 610
Cdd:PTZ00121 1665 EEAKKAEEdkkkAEEAKKAEEDEKKAAEALKKEAEEA 1701
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
513-613 3.91e-03

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: 39.66  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055 513 SKEIEKLRTSIQTLCKSalPLGKIMDYiQEDVDAMQNELQMWHSENRQHAEALQQ------------EQRITDCAVEPLK 580
Cdd:cd22656  109 DEELEEAKKTIKALLDD--LLKEAKKY-QDKAAKVVDKLTDFENQTEKDQTALETlekalkdlltdeGGAIARKEIKDLQ 185
                         90       100       110
                 ....*....|....*....|....*....|....
gi 578804055 581 AELAEL-EQLIKDQQDKICAVKANILKNEEKIQK 613
Cdd:cd22656  186 KELEKLnEEYAAKLKAKIDELKALIADDEAKLAA 219
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
230-354 6.80e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 39.52  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804055  230 RQKDRgNRERDRDSERKKETERKSEggkekerlrdrdrerdrdKGKDRDRRRVKNGEHSWDLDREKNREHDK---PEKKS 306
Cdd:TIGR01622   1 RYRDR-ERERLRDSSSAGDRDRRRD------------------KGRERSRDRSRDRERSRSRRRDRHRDRDYyrgRERRS 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578804055  307 ASSGEMSKKLSDGTFKDSKAETETEISTRASKSLTTKTSKRRSKNSVE 354
Cdd:TIGR01622  62 RSRRPNRRYRPREKRRRRGDSYRRRRDDRRSRREKPRARDGTPEPLTE 109
 
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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