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Conserved domains on  [gi|2054341318|emb|CAG2185842|]
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unnamed protein product [Mytilus edulis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zn-C2H2_CALCOCO1_TAX1BP1_like cd21965
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 498-520 7.68e-06

autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


:

Pssm-ID: 412012  Cd Length: 24  Bit Score: 42.56  E-value: 7.68e-06
                          10        20
                  ....*....|....*....|....
gi 2054341318 498 CPVCSRQFP-NMPMEDFQQHVFEC 520
Cdd:cd21965     1 CPICNKQFPpQVDQEAFEDHVESH 24
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-304 1.89e-05

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.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  45 QAYEDMKRRHQQVKSQNDILQQTIRDME---YSRQSTRNNSNMFGAagpvgaspgaDQDDQMAQVKAQIGYAES----VQ 117
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRE----------SLETQLKVLSRSINKIKQnleqKQ 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 118 RQLMRAQAKIITLENENKDLKNKLQSLiynknNTGQSNLIEKNTDLNSKNIQLSEKINTLNRDILTFKQLLQERDIQLQQ 197
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDL-----TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI 563

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 198 LEKQKDPNIMTEPFTrkiqELKTEMRDKDEHISALMERLKTVSKGYEQKIMTISDRewpesgyntrmnEDQTLLTVEESK 277
Cdd:TIGR04523 564 DEKNKEIEELKQTQK----SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL------------EKELEKAKKENE 627

                         250       260       270
                  ....*....|....*....|....*....|
gi 2054341318 278 QILFEIDK---HKKTLKQFLQQLKIQTETI 304
Cdd:TIGR04523 628 KLSSIIKNiksKKNKLKQEVKQIKETIKEI 657
Zn-C2H2_CALCOCO1_TAX1BP1_like super family cl41777
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 545-572 3.02e-05

autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


The actual alignment was detected with superfamily member cd21971:

Pssm-ID: 425408  Cd Length: 30  Bit Score: 40.97  E-value: 3.02e-05
                          10        20
                  ....*....|....*....|....*...
gi 2054341318 545 DRICPMCNKSFANTLPLADFEKHVQDHF 572
Cdd:cd21971     1 ERTCPMCGKQFSDQVSFHEFREHVEMHF 28
 
Name Accession Description Interval E-value
Zn-C2H2_CALCOCO1_TAX1BP1_like cd21965
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 498-520 7.68e-06

autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 412012  Cd Length: 24  Bit Score: 42.56  E-value: 7.68e-06
                          10        20
                  ....*....|....*....|....
gi 2054341318 498 CPVCSRQFP-NMPMEDFQQHVFEC 520
Cdd:cd21965     1 CPICNKQFPpQVDQEAFEDHVESH 24
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-304 1.89e-05

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: 47.71  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  45 QAYEDMKRRHQQVKSQNDILQQTIRDME---YSRQSTRNNSNMFGAagpvgaspgaDQDDQMAQVKAQIGYAES----VQ 117
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRE----------SLETQLKVLSRSINKIKQnleqKQ 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 118 RQLMRAQAKIITLENENKDLKNKLQSLiynknNTGQSNLIEKNTDLNSKNIQLSEKINTLNRDILTFKQLLQERDIQLQQ 197
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDL-----TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI 563

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 198 LEKQKDPNIMTEPFTrkiqELKTEMRDKDEHISALMERLKTVSKGYEQKIMTISDRewpesgyntrmnEDQTLLTVEESK 277
Cdd:TIGR04523 564 DEKNKEIEELKQTQK----SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL------------EKELEKAKKENE 627

                         250       260       270
                  ....*....|....*....|....*....|
gi 2054341318 278 QILFEIDK---HKKTLKQFLQQLKIQTETI 304
Cdd:TIGR04523 628 KLSSIIKNiksKKNKLKQEVKQIKETIKEI 657
Zn-C2H2_spn-F cd21971
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ...
 545-572 3.02e-05

C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar proteins; spn-F is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. It acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F is a coil-coiled protein containing a C2H2-type zinc binding domain.


Pssm-ID: 412017  Cd Length: 30  Bit Score: 40.97  E-value: 3.02e-05
                          10        20
                  ....*....|....*....|....*...
gi 2054341318 545 DRICPMCNKSFANTLPLADFEKHVQDHF 572
Cdd:cd21971     1 ERTCPMCGKQFSDQVSFHEFREHVEMHF 28
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 48-320 3.08e-05

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: 47.12  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  48 EDMKRRHQ-QVKSQNDILQQTIRDMEYSRQST--RNNS------NMFGAAGPVGASPGADQDDQMA-------------- 104
Cdd:pfam10174 213 EELHRRNQlQPDPAKTKALQTVIEMKDTKISSleRNIRdledevQMLKTNGLLHTEDREEEIKQMEvykshskfmknkid 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 105 QVKAQIGYAESvqrQLMRAQAKIITLENENKDLKNKLQSLIYN------KNNTGQS-------NLIEKNTDLNSKNIQL- 170
Cdd:pfam10174 293 QLKQELSKKES---ELLALQTKLETLTNQNSDCKQHIEVLKESltakeqRAAILQTevdalrlRLEEKESFLNKKTKQLq 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 171 --SEKINTLNRDILTFKQLLQERDIQLQQLEKqkdpnimtepftrKIQELKTEMRDKDEHISALMERLKTvskgyeqkIM 248
Cdd:pfam10174 370 dlTEEKSTLAGEIRDLKDMLDVKERKINVLQK-------------KIENLQEQLRDKDKQLAGLKERVKS--------LQ 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 249 TISDrewpesgyntrmNEDQTLLTVEES-------------------KQILFEIDKHKKTLKQFLQQLKIQTETIQKQGH 309
Cdd:pfam10174 429 TDSS------------NTDTALTTLEEAlsekeriierlkeqreredRERLEELESLKKENKDLKEKVSALQPELTEKES 496

                         330
                  ....*....|.
gi 2054341318 310 IIQDLKRRAVS 320
Cdd:pfam10174 497 SLIDLKEHASS 507
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 114-246 5.22e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 114 ESVQRQLMRAQA---KIITLENENKDLKNKLQSLiynknntgQSNLIEKNTDLNSKNIQLSE---KINTLNRDILTFKQL 187
Cdd:COG1579     3 PEDLRALLDLQEldsELDRLEHRLKELPAELAEL--------EDELAALEARLEAAKTELEDlekEIKRLELEIEEVEAR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2054341318 188 LQERDIQLQQLEKQKDPNIMTepftRKIQELKTEMRDKDEHISALMERLKTVSKGYEQK 246
Cdd:COG1579    75 IKKYEEQLGNVRNNKEYEALQ----KEIESLKRRISDLEDEILELMERIEELEEELAEL 129
Zn-C2H2_12 pfam18112
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ...
 546-572 8.69e-04

Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 407946  Cd Length: 27  Bit Score: 36.85  E-value: 8.69e-04
                          10        20
                  ....*....|....*....|....*..
gi 2054341318 546 RICPMCNKSFANTLPLADFEKHVQDHF 572
Cdd:pfam18112   1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
 
Name Accession Description Interval E-value
Zn-C2H2_CALCOCO1_TAX1BP1_like cd21965
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 498-520 7.68e-06

autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 412012  Cd Length: 24  Bit Score: 42.56  E-value: 7.68e-06
                          10        20
                  ....*....|....*....|....
gi 2054341318 498 CPVCSRQFP-NMPMEDFQQHVFEC 520
Cdd:cd21965     1 CPICNKQFPpQVDQEAFEDHVESH 24
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-304 1.89e-05

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: 47.71  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  45 QAYEDMKRRHQQVKSQNDILQQTIRDME---YSRQSTRNNSNMFGAagpvgaspgaDQDDQMAQVKAQIGYAES----VQ 117
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRE----------SLETQLKVLSRSINKIKQnleqKQ 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 118 RQLMRAQAKIITLENENKDLKNKLQSLiynknNTGQSNLIEKNTDLNSKNIQLSEKINTLNRDILTFKQLLQERDIQLQQ 197
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDL-----TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI 563

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 198 LEKQKDPNIMTEPFTrkiqELKTEMRDKDEHISALMERLKTVSKGYEQKIMTISDRewpesgyntrmnEDQTLLTVEESK 277
Cdd:TIGR04523 564 DEKNKEIEELKQTQK----SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL------------EKELEKAKKENE 627

                         250       260       270
                  ....*....|....*....|....*....|
gi 2054341318 278 QILFEIDK---HKKTLKQFLQQLKIQTETI 304
Cdd:TIGR04523 628 KLSSIIKNiksKKNKLKQEVKQIKETIKEI 657
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 117-306 2.93e-05

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: 46.94  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 117 QRQLMRAQAKIITLENENKDLKNKLQSLiynkNNTGQSNLI-----------EKNTDLNSKNIQLSEKINTLNRDI---- 181
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDL----NNQKEQDWNkelkselknqeKKLEEIQNQISQNNKIISQLNEQIsqlk 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 182 ----------LTFKQLLQERDIQLQQLEKQKDPNIMT-EPFTRKIQELKTEMRDKDEHISALMERLKTVSKGYEQKIM-- 248
Cdd:TIGR04523 349 keltnsesenSEKQRELEEKQNEIEKLKKENQSYKQEiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKei 428

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2054341318 249 ------------TISDREWPESGYNTRMNEDQTLLTVEES--KQILFEIDKHKKTLKQFLQQLKIQTETIQK 306
Cdd:TIGR04523 429 erlketiiknnsEIKDLTNQDSVKELIIKNLDNTRESLETqlKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
Zn-C2H2_spn-F cd21971
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ...
 545-572 3.02e-05

C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar proteins; spn-F is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. It acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F is a coil-coiled protein containing a C2H2-type zinc binding domain.


Pssm-ID: 412017  Cd Length: 30  Bit Score: 40.97  E-value: 3.02e-05
                          10        20
                  ....*....|....*....|....*...
gi 2054341318 545 DRICPMCNKSFANTLPLADFEKHVQDHF 572
Cdd:cd21971     1 ERTCPMCGKQFSDQVSFHEFREHVEMHF 28
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 48-320 3.08e-05

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: 47.12  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  48 EDMKRRHQ-QVKSQNDILQQTIRDMEYSRQST--RNNS------NMFGAAGPVGASPGADQDDQMA-------------- 104
Cdd:pfam10174 213 EELHRRNQlQPDPAKTKALQTVIEMKDTKISSleRNIRdledevQMLKTNGLLHTEDREEEIKQMEvykshskfmknkid 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 105 QVKAQIGYAESvqrQLMRAQAKIITLENENKDLKNKLQSLIYN------KNNTGQS-------NLIEKNTDLNSKNIQL- 170
Cdd:pfam10174 293 QLKQELSKKES---ELLALQTKLETLTNQNSDCKQHIEVLKESltakeqRAAILQTevdalrlRLEEKESFLNKKTKQLq 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 171 --SEKINTLNRDILTFKQLLQERDIQLQQLEKqkdpnimtepftrKIQELKTEMRDKDEHISALMERLKTvskgyeqkIM 248
Cdd:pfam10174 370 dlTEEKSTLAGEIRDLKDMLDVKERKINVLQK-------------KIENLQEQLRDKDKQLAGLKERVKS--------LQ 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 249 TISDrewpesgyntrmNEDQTLLTVEES-------------------KQILFEIDKHKKTLKQFLQQLKIQTETIQKQGH 309
Cdd:pfam10174 429 TDSS------------NTDTALTTLEEAlsekeriierlkeqreredRERLEELESLKKENKDLKEKVSALQPELTEKES 496

                         330
                  ....*....|.
gi 2054341318 310 IIQDLKRRAVS 320
Cdd:pfam10174 497 SLIDLKEHASS 507
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 124-307 3.22e-05

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: 46.94  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 124 QAKIITLENENKDLKNKLQSL---------IYNKNNTGQSNLIEKNTDLNSkniQLSEKINTL---NRDILTFKQLLQER 191
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKqqeinekttEISNTQTQLNQLKDEQNKIKK---QLSEKQKELeqnNKKIKELEKQLNQL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 192 DIQLQQLEKQKDPNIMTEPFT------RKIQELKTEMRDKDEHISALMERLKTVSKgyeqkimTISDREWPESGYNTRMN 265
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSelknqeKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELE 366

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2054341318 266 EDQTLLtveesKQILFEIDKHKKTLKQFLQQLKIQTETIQKQ 307
Cdd:TIGR04523 367 EKQNEI-----EKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 114-315 7.35e-05

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: 45.78  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 114 ESVQRQLMRAQAKIITLENENKDLKNKLQSLiynkNNtgQSNLIEKN-TDLNSKNIQLSEKINTLNRDILTF-------K 185
Cdd:TIGR04523  43 KTIKNELKNKEKELKNLDKNLNKDEEKINNS----NN--KIKILEQQiKDLNDKLKKNKDKINKLNSDLSKInseikndK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 186 QLLQERDIQLQQLEKQKDPN------IMTEpFTRKIQELK---TEMRDKDEHISALMERLKTVSKGYEQKIMTISDREWP 256
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENkknidkFLTE-IKKKEKELEklnNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2054341318 257 ESGYNTRM------NEDQTLLT--VEESKQILFEIDKHKKTLKQFLQQLKIQTETIQKQghiIQDLK 315
Cdd:TIGR04523 196 LLKLELLLsnlkkkIQKNKSLEsqISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---LNQLK 259
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-293 9.76e-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: 45.43  E-value: 9.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318   33 EENPQASHHALFQAYEDMKRRHQQVKSQNDILQQTIRDMEYSRQSTRNNSNMFGAAGPVGASPGADQDDQMAQVKAQIgy 112
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-- 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  113 aESVQRQLMRAQAKIITLENENKDLKNKLQSLIYNKNNTGQSNlieknTDLNSKNIQLSEKINTLNRDILTFKQLLQERD 192
Cdd:TIGR02168  799 -KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL-----EDLEEQIEELSEDIESLAAEIEELEELIEELE 872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  193 IQLQQLEKQKDP---NIMT-----EPFTRKIQELKTEMRDKDEHISALMERLKTVS---KGYEQKIMTISDREWPEsgYN 261
Cdd:TIGR02168  873 SELEALLNERASleeALALlrselEELSEELRELESKRSELRRELEELREKLAQLElrlEGLEVRIDNLQERLSEE--YS 950

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2054341318  262 TRMNEDQTL--LTVEESKQILFEIDKHKKTLKQF 293
Cdd:TIGR02168  951 LTLEEAEALenKIEDDEEEARRRLKRLENKIKEL 984
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-306 1.59e-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: 44.63  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 101 DQMAQVKAQIgyaESVQRQLMRAQAKIITLENENKDLKNKLQSLiYNKNNTGQSNLIEKNTDL---------NSKNIQ-L 170
Cdd:TIGR04523 314 SELKNQEKKL---EEIQNQISQNNKIISQLNEQISQLKKELTNS-ESENSEKQRELEEKQNEIeklkkenqsYKQEIKnL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 171 SEKINTLNRDILTFKQLLQERDIQLQQLEKQKdpnimtEPFTRKIQELKTEMRDKDEHISAL----------MERLKTVS 240
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEK------ELLEKEIERLKETIIKNNSEIKDLtnqdsvkeliIKNLDNTR 463

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 241 KGYEQKIMTISDrewpeSGYNTRMNEDQTLLTVEESKQILFEIDKHKKTLKQFLQQLKIQ----TETIQK 306
Cdd:TIGR04523 464 ESLETQLKVLSR-----SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKisslKEKIEK 528
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 114-246 5.22e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 114 ESVQRQLMRAQA---KIITLENENKDLKNKLQSLiynknntgQSNLIEKNTDLNSKNIQLSE---KINTLNRDILTFKQL 187
Cdd:COG1579     3 PEDLRALLDLQEldsELDRLEHRLKELPAELAEL--------EDELAALEARLEAAKTELEDlekEIKRLELEIEEVEAR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2054341318 188 LQERDIQLQQLEKQKDPNIMTepftRKIQELKTEMRDKDEHISALMERLKTVSKGYEQK 246
Cdd:COG1579    75 IKKYEEQLGNVRNNKEYEALQ----KEIESLKRRISDLEDEILELMERIEELEEELAEL 129
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 39-298 5.61e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318   39 SHHALFQayeDMKRRH-QQVKSQNDILQQTIR---DMEYSRQSTRNNSNMFgaAGPVGASPGADQDDQMAQVKAQIgyae 114
Cdd:pfam01576  342 SHEAQLQ---EMRQKHtQALEELTEQLEQAKRnkaNLEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEG---- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  115 svqrQLMRAQAKIITLENENKDLKNKLQSLiynknntgQSNLIEKNTDLN---SKNIQLSEKINTLNRDILTFKQLLQER 191
Cdd:pfam01576  413 ----QLQELQARLSESERQRAELAEKLSKL--------QSELESVSSLLNeaeGKNIKLSKDVSSLESQLQDTQELLQEE 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  192 DIQ-------LQQLEKQKDpNIM---------TEPFTRKIQELK---TEMRDKDEHISALMERLKTVSKGYEQKIMTISD 252
Cdd:pfam01576  481 TRQklnlstrLRQLEDERN-SLQeqleeeeeaKRNVERQLSTLQaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2054341318  253 R-EWPESGY------NTRMNE--DQTLLTVEESKQILFEIDKHKKTLKQFLQQLK 298
Cdd:pfam01576  560 QlEEKAAAYdklektKNRLQQelDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEK 614
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 91-328 6.34e-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: 42.44  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  91 VGASPGADQDDQMAQVKAQIgyaESVQRQLMRAQAKIITLENENKDLKNKLQsliynknntgqsnliekntDLNSKNIQL 170
Cdd:COG4942    10 LLALAAAAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLA-------------------ALERRIAAL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 171 SEKINTLNRDILTFKQLLQERDIQLQQLEKQKD---------------------PNIMTEP-----FTRKIQELKTEMRD 224
Cdd:COG4942    68 ARRIRALEQELAALEAELAELEKEIAELRAELEaqkeelaellralyrlgrqppLALLLSPedfldAVRRLQYLKYLAPA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 225 KDEHISALMERLKTVSkgyEQKIMTISDREWPESGYNTRMNEDQTLLT-VEESKQILFEIDKHKKTLKQFLQQLKIQTET 303
Cdd:COG4942   148 RREQAEELRADLAELA---ALRAELEAERAELEALLAELEEERAALEAlKAERQKLLARLEKELAELAAELAELQQEAEE 224

                         250       260
                  ....*....|....*....|....*.
gi 2054341318 304 IQKQ-GHIIQDLKRRAVSTNNIRVPA 328
Cdd:COG4942   225 LEALiARLEAEAAAAAERTPAAGFAA 250
Zn-C2H2_12 pfam18112
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ...
 546-572 8.69e-04

Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 407946  Cd Length: 27  Bit Score: 36.85  E-value: 8.69e-04
                          10        20
                  ....*....|....*....|....*..
gi 2054341318 546 RICPMCNKSFANTLPLADFEKHVQDHF 572
Cdd:pfam18112   1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
Zn-C2H2_CALCOCO1_TAX1BP1_like cd21965
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 548-571 1.12e-03

autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 412012  Cd Length: 24  Bit Score: 36.40  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|....
gi 2054341318 548 CPMCNKSFANTLPLADFEKHVQDH 571
Cdd:cd21965     1 CPICNKQFPPQVDQEAFEDHVESH 24
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
135-316 2.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 135 KDLKNKLQSLIYNKNNTGQSNL---------IEKNTDLNSKNIQLSEKINTLNRDILTFKQLLQERDIQLQQLEKQKDPn 205
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLkelkeleeeLKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 206 imtEPFTRKIQELKTEMRDKDEHISALMERLKTVS------KGYEQKIMTIS---DREWPESGYNTRMNEDQTLLTVEES 276
Cdd:COG4717   128 ---LPLYQELEALEAELAELPERLEELEERLEELReleeelEELEAELAELQeelEELLEQLSLATEEELQDLAEELEEL 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2054341318 277 KQILFEIDKHKKTLKQFLQQLKIQTETIQKQGHIIQDLKR 316
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Zn-C2H2_TAX1BP1_rpt2 cd21970
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ...
 546-572 2.28e-03

second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.


Pssm-ID: 412016  Cd Length: 27  Bit Score: 35.61  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|....*..
gi 2054341318 546 RICPMCNKSFANTLPLADFEKHVQDHF 572
Cdd:cd21970     1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
105-312 2.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 105 QVKAQIGYAESVQRQLMRAQAKIITLENENKDLKNKLQSLiynknntgQSNLIEKNTDLNSKNIQLSEKINTLNRdiltF 184
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA--------RSELEQLEEELEELNEQLQAAQAELAQ----A 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 185 KQLLQERDIQLQQLEKQkdpnimtepftrkIQELKTEMRDKDEHISALMERLKTVSKGYEQKIMTISDREwpesgynTRM 264
Cdd:COG4372   100 QEELESLQEEAEELQEE-------------LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE-------EQL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2054341318 265 NEDQTLLTVEESKQILFEIDKHKKTLKQFLQQLKIQTETIQKQGHIIQ 312
Cdd:COG4372   160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 102-237 2.46e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.83  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 102 QMAQVKAQIgyaESVQRQLMRAQAKIITLENENK-------DLKNKLQSLiyNKNNTGQSNLIEKNTDLNSKNIQLSEKI 174
Cdd:pfam05622 298 QEGSYRERL---TELQQLLEDANRRKNELETQNRlanqrilELQQQVEEL--QKALQEQGSKAEDSSLLKQKLEEHLEKL 372

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2054341318 175 NTLNRDiltfkqlLQERDIQLQQLEkqkdPNIMTEPfTRKIQELKTEMRDKDEHISALMERLK 237
Cdd:pfam05622 373 HEAQSE-------LQKKKEQIEELE----PKQDSNL-AQKIDELQEALRKKDEDMKAMEERYK 423
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 103-245 2.79e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.44  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 103 MAQVKAQigyAESVQRQLMRAQAKIITLENENKDLKNKLQSLiynknntgqsnliekntdlNSKNIQLSEKINTLNRDIL 182
Cdd:pfam12718   2 MNSLKLE---AENAQERAEELEEKVKELEQENLEKEQEIKSL-------------------THKNQQLEEEVEKLEEQLK 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2054341318 183 TFKQLLQERdiqlqqlEKQKDPNimtEPFTRKIQELKTEMRDKDEHISALMERLKTVSKGYEQ 245
Cdd:pfam12718  60 EAKEKAEES-------EKLKTNN---ENLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEH 112
Zn-C2H2_TAX1BP1_rpt1 cd21969
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ...
 548-571 3.00e-03

first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.


Pssm-ID: 412015  Cd Length: 24  Bit Score: 35.47  E-value: 3.00e-03
                          10        20
                  ....*....|....*....|....
gi 2054341318 548 CPMCNKSFANTLPLADFEKHVQDH 571
Cdd:cd21969     1 CPLCELVFPPNYDQSKFEQHVESH 24
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 87-250 3.59e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.40  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  87 AAGPVGASPGADQDDQMAQVKAQIgyaESVQRQLMRAQAKIITLENENKDLKNKLQSLIYNKNNTGQSNLI-EKNTDLNS 165
Cdd:pfam05667 314 AATSSPPTKVETEEELQQQREEEL---EELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEElEKQYKVKK 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 166 KNIQL----SEKINTLNRDIltfkQLLQERDIQL-QQLEKQKDPNIM---------------TEPFTRKIQELKTEMRD- 224
Cdd:pfam05667 391 KTLDLlpdaEENIAKLQALV----DASAQRLVELaGQWEKHRVPLIEeyralkeaksnkedeSQRKLEEIKELREKIKEv 466

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2054341318 225 ------KDEHISALMERLKTVSKG-----YEQKIMTI 250
Cdd:pfam05667 467 aeeakqKEELYKQLVAEYERLPKDvsrsaYTRRILEI 503
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-316 4.75e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  113 AESVQRQLMRAQAKIITLENENKDLKnKLQSLIyNKNNTGQSNLIEKNTDLNSKNIQLSEKINTLNRDILTFKQLLQER- 191
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLA-ALEEQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAe 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  192 -----------DIQLQQLEKQKDPNIMTEPFTRKIQELKTEMRDKDEHISALMERLKtvskgyeqkimtisdREWPESGY 260
Cdd:COG4913    741 dlarlelrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN---------------REWPAETA 805

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2054341318  261 NTrmneDQTLLTVEESKQILFEIDKHKktLKQFLQQLK--IQTETIQKQGHIIQDLKR 316
Cdd:COG4913    806 DL----DADLESLPEYLALLDRLEEDG--LPEYEERFKelLNENSIEFVADLLSKLRR 857
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-318 5.09e-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: 40.04  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  117 QRQLMRAQAKIITLENenkDLKNKlQSLIYNKNNTGQSNLIEKNTDLNskniQLSEKINTLNRDILTFKQLLQERDIQLQ 196
Cdd:TIGR02168  637 LAKKLRPGYRIVTLDG---DLVRP-GGVITGGSAKTNSSILERRREIE----ELEEKIEELEEKIAELEKALAELRKELE 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  197 QLEKQkdpnimTEPFTRKIQELKTEMRDKDEHISALMERLKTVSKGYEQKIMTISDREWPESGYNTRMNEDQTLLTVEES 276
Cdd:TIGR02168  709 ELEEE------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2054341318  277 kqilfEIDKHKKTLKQFLQQLKIQTETIQKQGHIIQDLKRRA 318
Cdd:TIGR02168  783 -----EIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 131-316 7.26e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  131 ENENKDLKNKLQSLIYNKNNTGQSNL----IEKNTDLNSKNIQ-----LSEKINTLNRDILTFKQLLQE----RDIQLQQ 197
Cdd:TIGR00618  679 QLALQKMQSEKEQLTYWKEMLAQCQTllreLETHIEEYDREFNeienaSSSLGSDLAAREDALNQSLKElmhqARTVLKA 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  198 LE---KQKDPNIMTEPFT-RKIQELKTEMRDKDEHISALMERLKTVSKGYEQK------IMTISDREWPEsgyntrmNED 267
Cdd:TIGR00618  759 RTeahFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdedILNLQCETLVQ-------EEE 831

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2054341318  268 QTLLTVEESKQILFEIDKHKKTLKQFLQQlkiQTETIQKQGHIIQDLKR 316
Cdd:TIGR00618  832 QFLSRLEEKSATLGEITHQLLKYEECSKQ---LAQLTQEQAKIIQLSDK 877
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 101-183 7.54e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 36.61  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 101 DQMAQVKAQIGYAESVQRQLMRAQAKIITLENENKDLKNKLQSLIyNKNNTGQS---NLIEKNTDLNSKNIQLSEKINTL 177
Cdd:pfam04871  22 AELQELSKQYNSLEQKESQAKELEAEVKKLEEALKKLKAELSEEK-QKEKEKQSeldDLLLLLGDLEEKVEKYKARLKEL 100


                  ....*.
gi 2054341318 178 NRDILT 183
Cdd:pfam04871 101 GEEVLS 106
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
105-238 8.59e-03

Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 39.33  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 105 QVKAQIGYAESVQRQLMRAQAKIITLENENKDLKNKLQSLIYNKNNTGQSNLIEKNTDLNSKNIQLSEKINTLNRDILTF 184
Cdd:COG3933   353 LLKLLLLLLLNERLLLLELKILIEPLDIFFDSSASSDESDESEEDENLYEIIEIKKKLLLELGIDEEEINIIIEIDIDVH 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2054341318 185 KQLLQERDIQL---QQLEKQKDPNImtEPFTRKIQE-----LKTEMRDKDE-----HISALMERLKT 238
Cdd:COG3933   433 LLKFIYDDNKNfnkEELAKIVDEDI--INVVEEILElaekkLGRKFSENFIyalslHLSSFIERIKE 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-322 8.63e-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: 39.27  E-value: 8.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  119 QLMRAQAKIITLENENKDLKNKLQSLiynknNTGQSNLIEKNTDLNSKNIQLSEKINTLNRDILTFKQLLQ--ERDIQLQ 196
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEEL-----TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrlEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318  197 QlEKQKDPNIMTEPFTRKIQELKtEMRDKDEHISALME----RLKTVSKGYEQKIMTiSDREWPESgyNTRMNEDQTLLT 272
Cdd:TIGR02168  308 R-ERLANLERQLEELEAQLEELE-SKLDELAEELAELEekleELKEELESLEAELEE-LEAELEEL--ESRLEELEEQLE 382

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2054341318  273 VEESK--QILFEIDKHKKTLKQFLQQLKIQTETIQKQGHIIQDLKRRAVSTN 322
Cdd:TIGR02168  383 TLRSKvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 172-258 9.94e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 38.72  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054341318 172 EKINTLNRDILTFKQLLQERDIQLQQLE----KQKDPNIMTEPFT-RKIQELKTEMR----DKDEHISALMERLKTVSKg 242
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKLEvelgREKDCNRVQLSESrRELQELKASLRvaqkEKEQLQAEKQELLEYIRQ- 396

                          90
                  ....*....|....*.
gi 2054341318 243 YEQKIMTISDREWPES 258
Cdd:pfam07888 397 LEQRLETVADAKWSEA 412
 
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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