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Conserved domains on  [gi|71996943|ref|NP_001022981|]
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JNK-interacting protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
41-195 2.73e-60

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


:

Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 202.85  E-value: 2.73e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     41 VQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKY 120
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71996943    121 IEIEDTLIGQNKELDKKIESLESIMRMLElkaknaTDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTK 195
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
818-1019 1.21e-42

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


The actual alignment was detected with superfamily member pfam19056:

Pssm-ID: 465964  Cd Length: 487  Bit Score: 163.27  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    818 PTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPD--AVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSAt 895
Cdd:pfam19056  102 PTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEPPKLVKLGVL- 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    896 sSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVD 975
Cdd:pfam19056  181 -PVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHTETLEHLQDIN 259
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 71996943    976 IEPYVTKMLGTSKldfsYMRTTALLVSNRRLWIGTGTGVIISVP 1019
Cdd:pfam19056  260 IATRVHFMLPGQK----RVSVTSLLICQGLLWVGTNLGVIVALP 299
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
332-400 2.87e-21

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


:

Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 88.52  E-value: 2.87e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71996943    332 MGREVENLIKENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIK 400
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
4-457 1.14e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.72  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943      4 NLSPVNEMADSITSSTpSEIVYGGPGSPDEHRTMSDKVQTMASAIYR---ELETmiKVHGEDGVKTLMPLVVNVLEAL-- 78
Cdd:pfam05483  283 NLKELIEKKDHLTKEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQlteEKEA--QMEELNKAKAAHSFVVTEFEATtc 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     79 DLAYLERDEQTaELE----MLKEDNEQLQTQYEREKALRKQTEQKYIEIED--TLIGQNKELDKKIESLESIMRMLELKA 152
Cdd:pfam05483  360 SLEELLRTEQQ-RLEknedQLKIITMELQKKSSELEEMTKFKNNKEVELEElkKILAEDEKLLDEKKQFEKIAEELKGKE 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    153 KNATdhaSRLEEREVE-QKLEFDRlherynTLLRTHVDHMERTKYLMGSEkfelMQNMPLPNMQLRNKMGMAAsvdassi 231
Cdd:pfam05483  439 QELI---FLLQAREKEiHDLEIQL------TAIKTSEEHYLKEVEDLKTE----LEKEKLKNIELTAHCDKLL------- 498
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    232 rgvsdLISAHMTQSTT-MDVNLANHitnedwQDEFSSDIEPSPRDIPQssadalTSPITTKEPTPKREAASPKQSEEEEA 310
Cdd:pfam05483  499 -----LENKELTQEASdMTLELKKH------QEDIINCKKQEERMLKQ------IENLEEKEMNLRDELESVREEFIQKG 561
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    311 DETT-SVDPKENNdllgadltGMGREVENLIKEnSELLDMKNALNIVKNDLINQ---VDELNSENMILRDENLSRQMVSE 386
Cdd:pfam05483  562 DEVKcKLDKSEEN--------ARSIEYEVLKKE-KQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLN 632
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996943    387 KMQEQITKHEEEIKTLKQKLMEKEN--EQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLMELEESIKWTEM 457
Cdd:pfam05483  633 AYEIKVNKLELELASAKQKFEEIIDnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEM 705
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
41-195 2.73e-60

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 202.85  E-value: 2.73e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     41 VQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKY 120
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71996943    121 IEIEDTLIGQNKELDKKIESLESIMRMLElkaknaTDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTK 195
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
818-1019 1.21e-42

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 163.27  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    818 PTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPD--AVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSAt 895
Cdd:pfam19056  102 PTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEPPKLVKLGVL- 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    896 sSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVD 975
Cdd:pfam19056  181 -PVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHTETLEHLQDIN 259
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 71996943    976 IEPYVTKMLGTSKldfsYMRTTALLVSNRRLWIGTGTGVIISVP 1019
Cdd:pfam19056  260 IATRVHFMLPGQK----RVSVTSLLICQGLLWVGTNLGVIVALP 299
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
332-400 2.87e-21

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 88.52  E-value: 2.87e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71996943    332 MGREVENLIKENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIK 400
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
41-108 7.24e-09

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 53.75  E-value: 7.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71996943   41 VQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYER 108
Cdd:cd14445   18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRLELEKRE 85
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
4-457 1.14e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.72  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943      4 NLSPVNEMADSITSSTpSEIVYGGPGSPDEHRTMSDKVQTMASAIYR---ELETmiKVHGEDGVKTLMPLVVNVLEAL-- 78
Cdd:pfam05483  283 NLKELIEKKDHLTKEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQlteEKEA--QMEELNKAKAAHSFVVTEFEATtc 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     79 DLAYLERDEQTaELE----MLKEDNEQLQTQYEREKALRKQTEQKYIEIED--TLIGQNKELDKKIESLESIMRMLELKA 152
Cdd:pfam05483  360 SLEELLRTEQQ-RLEknedQLKIITMELQKKSSELEEMTKFKNNKEVELEElkKILAEDEKLLDEKKQFEKIAEELKGKE 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    153 KNATdhaSRLEEREVE-QKLEFDRlherynTLLRTHVDHMERTKYLMGSEkfelMQNMPLPNMQLRNKMGMAAsvdassi 231
Cdd:pfam05483  439 QELI---FLLQAREKEiHDLEIQL------TAIKTSEEHYLKEVEDLKTE----LEKEKLKNIELTAHCDKLL------- 498
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    232 rgvsdLISAHMTQSTT-MDVNLANHitnedwQDEFSSDIEPSPRDIPQssadalTSPITTKEPTPKREAASPKQSEEEEA 310
Cdd:pfam05483  499 -----LENKELTQEASdMTLELKKH------QEDIINCKKQEERMLKQ------IENLEEKEMNLRDELESVREEFIQKG 561
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    311 DETT-SVDPKENNdllgadltGMGREVENLIKEnSELLDMKNALNIVKNDLINQ---VDELNSENMILRDENLSRQMVSE 386
Cdd:pfam05483  562 DEVKcKLDKSEEN--------ARSIEYEVLKKE-KQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLN 632
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996943    387 KMQEQITKHEEEIKTLKQKLMEKEN--EQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLMELEESIKWTEM 457
Cdd:pfam05483  633 AYEIKVNKLELELASAKQKFEEIIDnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEM 705
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
88-186 2.48e-05

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: 47.84  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   88 QTAELEMLKEDNEQLQTQYEREKALRKQTEQKyieiEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREV 167
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                         90
                 ....*....|....*....
gi 71996943  168 EQKLEFDRLHERYNTLLRT 186
Cdd:COG4942   94 ELRAELEAQKEELAELLRA 112
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
112-453 3.18e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    112 LRKQTEQKYIEIEdTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDhm 191
Cdd:TIGR04523  361 KQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK-- 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    192 ertkylmgsekfelmqnmplpnmqlrnkmgmaasvDASSIrgvSDLISahmtQSTTMDVNLANHITNEDWQDEFSSDIEP 271
Cdd:TIGR04523  438 -----------------------------------NNSEI---KDLTN----QDSVKELIIKNLDNTRESLETQLKVLSR 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    272 SPRDIPQSSaDALTSPITTKEPTPKREAASPKQSEEEEADETTSVDP-KENNDLLGADLTgmgrEVENLIKE-NSELLDM 349
Cdd:TIGR04523  476 SINKIKQNL-EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlKEKIEKLESEKK----EKESKISDlEDELNKD 550
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    350 KNALNivKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEKENEQE--EDDVPMAMRKrft 427
Cdd:TIGR04523  551 DFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISslEKELEKAKKE--- 625
                          330       340
                   ....*....|....*....|....*.
gi 71996943    428 RSEMQRVLMDRNAYKEKLMELEESIK 453
Cdd:TIGR04523  626 NEKLSSIIKNIKSKKNKLKQEVKQIK 651
PRK00106 PRK00106
ribonuclease Y;
84-178 2.71e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 41.78  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    84 ERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLE 163
Cdd:PRK00106   63 KRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHID 142
                          90
                  ....*....|....*.
gi 71996943   164 EREVE-QKLEFDRLHE 178
Cdd:PRK00106  143 EREEQvEKLEEQKKAE 158
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
341-409 3.40e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 3.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71996943  341 KENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEK 409
Cdd:cd22887   11 KRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAK 79
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
70-416 9.20e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   70 LVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLE 149
Cdd:COG4372   25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  150 LKAKNATDHASRLEEREVEQKL---EFDRLHERYNTLLRTHVDHMERTKYLMgSEKFELMQNMPLPNMQLRNKMgmaasv 226
Cdd:COG4372  105 SLQEEAEELQEELEELQKERQDleqQRKQLEAQIAELQSEIAEREEELKELE-EQLESLQEELAALEQELQALS------ 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  227 DASSIRGVSDLISAHMTQSTTMDVNLANHITNEDWQDEFSS-DIEPSPRDIPQSSADALTSPITTKEPTPKREAASPKQS 305
Cdd:COG4372  178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEeLLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  306 EEEEADETTSVDPKENNDLLGADLTGMGREVENLIKENSELLDM-KNALNIVKNDLINQVDELNSENMILRDENLSRQMV 384
Cdd:COG4372  258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLlNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
                        330       340       350
                 ....*....|....*....|....*....|..
gi 71996943  385 SEKMQEQITKHEEEIKTLKQKLMEKENEQEED 416
Cdd:COG4372  338 ELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
84-185 9.73e-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: 9.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     84 ERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDtligQNKELDKKIESLESIMRMLELKAKNATDHASRLE 163
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES----RLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                           90       100
                   ....*....|....*....|..
gi 71996943    164 EREVEQKLEFDRLHERYNTLLR 185
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLK 428
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
41-195 2.73e-60

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 202.85  E-value: 2.73e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     41 VQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKY 120
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71996943    121 IEIEDTLIGQNKELDKKIESLESIMRMLElkaknaTDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTK 195
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
818-1019 1.21e-42

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 163.27  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    818 PTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPD--AVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSAt 895
Cdd:pfam19056  102 PTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEPPKLVKLGVL- 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    896 sSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVD 975
Cdd:pfam19056  181 -PVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHTETLEHLQDIN 259
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 71996943    976 IEPYVTKMLGTSKldfsYMRTTALLVSNRRLWIGTGTGVIISVP 1019
Cdd:pfam19056  260 IATRVHFMLPGQK----RVSVTSLLICQGLLWVGTNLGVIVALP 299
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
332-400 2.87e-21

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 88.52  E-value: 2.87e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71996943    332 MGREVENLIKENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIK 400
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
41-108 7.24e-09

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 53.75  E-value: 7.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71996943   41 VQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYER 108
Cdd:cd14445   18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRLELEKRE 85
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
4-457 1.14e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.72  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943      4 NLSPVNEMADSITSSTpSEIVYGGPGSPDEHRTMSDKVQTMASAIYR---ELETmiKVHGEDGVKTLMPLVVNVLEAL-- 78
Cdd:pfam05483  283 NLKELIEKKDHLTKEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQlteEKEA--QMEELNKAKAAHSFVVTEFEATtc 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     79 DLAYLERDEQTaELE----MLKEDNEQLQTQYEREKALRKQTEQKYIEIED--TLIGQNKELDKKIESLESIMRMLELKA 152
Cdd:pfam05483  360 SLEELLRTEQQ-RLEknedQLKIITMELQKKSSELEEMTKFKNNKEVELEElkKILAEDEKLLDEKKQFEKIAEELKGKE 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    153 KNATdhaSRLEEREVE-QKLEFDRlherynTLLRTHVDHMERTKYLMGSEkfelMQNMPLPNMQLRNKMGMAAsvdassi 231
Cdd:pfam05483  439 QELI---FLLQAREKEiHDLEIQL------TAIKTSEEHYLKEVEDLKTE----LEKEKLKNIELTAHCDKLL------- 498
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    232 rgvsdLISAHMTQSTT-MDVNLANHitnedwQDEFSSDIEPSPRDIPQssadalTSPITTKEPTPKREAASPKQSEEEEA 310
Cdd:pfam05483  499 -----LENKELTQEASdMTLELKKH------QEDIINCKKQEERMLKQ------IENLEEKEMNLRDELESVREEFIQKG 561
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    311 DETT-SVDPKENNdllgadltGMGREVENLIKEnSELLDMKNALNIVKNDLINQ---VDELNSENMILRDENLSRQMVSE 386
Cdd:pfam05483  562 DEVKcKLDKSEEN--------ARSIEYEVLKKE-KQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLN 632
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996943    387 KMQEQITKHEEEIKTLKQKLMEKEN--EQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLMELEESIKWTEM 457
Cdd:pfam05483  633 AYEIKVNKLELELASAKQKFEEIIDnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEM 705
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
88-186 2.48e-05

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: 47.84  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   88 QTAELEMLKEDNEQLQTQYEREKALRKQTEQKyieiEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREV 167
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                         90
                 ....*....|....*....
gi 71996943  168 EQKLEFDRLHERYNTLLRT 186
Cdd:COG4942   94 ELRAELEAQKEELAELLRA 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
77-179 1.47e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   77 ALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTL---IGQNKELDKKIESLESIMRMLELKAK 153
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEERRR 312
                         90       100
                 ....*....|....*....|....*.
gi 71996943  154 NATDHASRLEEREVEQKLEFDRLHER 179
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEE 338
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
112-453 3.18e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    112 LRKQTEQKYIEIEdTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDhm 191
Cdd:TIGR04523  361 KQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK-- 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    192 ertkylmgsekfelmqnmplpnmqlrnkmgmaasvDASSIrgvSDLISahmtQSTTMDVNLANHITNEDWQDEFSSDIEP 271
Cdd:TIGR04523  438 -----------------------------------NNSEI---KDLTN----QDSVKELIIKNLDNTRESLETQLKVLSR 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    272 SPRDIPQSSaDALTSPITTKEPTPKREAASPKQSEEEEADETTSVDP-KENNDLLGADLTgmgrEVENLIKE-NSELLDM 349
Cdd:TIGR04523  476 SINKIKQNL-EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlKEKIEKLESEKK----EKESKISDlEDELNKD 550
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    350 KNALNivKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEKENEQE--EDDVPMAMRKrft 427
Cdd:TIGR04523  551 DFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISslEKELEKAKKE--- 625
                          330       340
                   ....*....|....*....|....*.
gi 71996943    428 RSEMQRVLMDRNAYKEKLMELEESIK 453
Cdd:TIGR04523  626 NEKLSSIIKNIKSKKNKLKQEVKQIK 651
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
91-415 5.86e-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: 44.24  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     91 ELEMLKEDNEQLQTQYEREKA--------LRKQTEQKY--IEIEDTLIGQNKELDKKIESLESimrmlelKAKNATDHAS 160
Cdd:TIGR04523  163 DLKKQKEELENELNLLEKEKLniqknidkIKNKLLKLEllLSNLKKKIQKNKSLESQISELKK-------QNNQLKDNIE 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    161 RLEEREVEQKLEFDRLHERYNTLLrthvDHMERTKYLMGSEKFELMQNmplpNMQLRNKmgmaasvdassirgvSDLIsa 240
Cdd:TIGR04523  236 KKQQEINEKTTEISNTQTQLNQLK----DEQNKIKKQLSEKQKELEQN----NKKIKEL---------------EKQL-- 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    241 hmtQSTTMDVNLANHITNEDWQDEFSSDIEPSPRDIPQssadaLTSPITTKEPTPKREAASPKQSEEEEADETTsvdpke 320
Cdd:TIGR04523  291 ---NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE-----IQNQISQNNKIISQLNEQISQLKKELTNSES------ 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    321 NNDLLGADLTGMGREVENLIKENSELLDMKNALNIVKNDL---INQVDELNSENMI----LRDENLSRQMVSEKMQEQIT 393
Cdd:TIGR04523  357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQKDEqikkLQQEKELLEKEIERLKETII 436
                          330       340
                   ....*....|....*....|..
gi 71996943    394 KHEEEIKTLKQKLMEKENEQEE 415
Cdd:TIGR04523  437 KNNSEIKDLTNQDSVKELIIKN 458
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
79-179 1.74e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   79 DLAYLER-DEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLiGQNKELDKKIESLESIMRMLELKAKNATD 157
Cdd:COG0542  435 DEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY-GKIPELEKELAELEEELAELAPLLREEVT 513
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 71996943  158 HA--------------SRLEEREVE--QKLEfDRLHER 179
Cdd:COG0542  514 EEdiaevvsrwtgipvGKLLEGEREklLNLE-EELHER 550
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
84-413 2.38e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     84 ERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDtligQNKELDKKIESLES--------IMRMLELKAKNA 155
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQekellekeIERLKETIIKNN 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    156 tDHASRLEEREVEQKLEFDRLhERYNTLLRTHVDHMERtkyLMGSEKFELMQNmplpNMQLRNKmgmaasvdassirgVS 235
Cdd:TIGR04523  440 -SEIKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR---SINKIKQNLEQK----QKELKSK--------------EK 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    236 DLISahMTQSTTmdvNLANHITN-EDWQDEFSSDIEpsprdipqssadALTSPITTKEptpkREAASPKQSEEEEADETT 314
Cdd:TIGR04523  497 ELKK--LNEEKK---ELEEKVKDlTKKISSLKEKIE------------KLESEKKEKE----SKISDLEDELNKDDFELK 555
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    315 SVDPKENNDLLGADLTGMGREVENLIKENSELLDMKNALNIVKNDLINQVdelnsENMILRDENLSRQMvsEKMQEQITK 394
Cdd:TIGR04523  556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-----EEKEKKISSLEKEL--EKAKKENEK 628
                          330
                   ....*....|....*....
gi 71996943    395 HEEEIKTLKQKLmEKENEQ 413
Cdd:TIGR04523  629 LSSIIKNIKSKK-NKLKQE 646
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
76-194 2.60e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   76 EALDLAYLER--DEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDtLIGQNKELDKKIESLE-----SIMRML 148
Cdd:COG4913  659 DEIDVASAEReiAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEeeldeLQDRLE 737
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71996943  149 ELKAKNATDHASRLEER-------EVEQKL--EFDRLHERYNTLLRTHVDHMERT 194
Cdd:COG4913  738 AAEDLARLELRALLEERfaaalgdAVERELreNLEERIDALRARLNRAEEELERA 792
PRK00106 PRK00106
ribonuclease Y;
84-178 2.71e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 41.78  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    84 ERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLE 163
Cdd:PRK00106   63 KRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHID 142
                          90
                  ....*....|....*.
gi 71996943   164 EREVE-QKLEFDRLHE 178
Cdd:PRK00106  143 EREEQvEKLEEQKKAE 158
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
341-409 3.40e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 3.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71996943  341 KENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEK 409
Cdd:cd22887   11 KRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAK 79
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-193 3.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   46 SAIYRELETMikvhgEDGVKTLMPLV------------VNVLEALDL------AYLERDEQTAELEMLKEDNEQLQTQYE 107
Cdd:COG4913  238 ERAHEALEDA-----REQIELLEPIRelaeryaaarerLAELEYLRAalrlwfAQRRLELLEAELEELRAELARLEAELE 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  108 REKALRKQTEQKYIEIEDTLIGQN----KELDKKIESLESIMRMLELKAKNATDHASRLEEREVEQKLEFDRLHERYNTL 183
Cdd:COG4913  313 RLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
                        170
                 ....*....|
gi 71996943  184 LRTHVDHMER 193
Cdd:COG4913  393 LEALEEELEA 402
Com_YlbF pfam06133
Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and ...
334-412 5.83e-03

Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and archaeal proteins that includes both YlbF and YmcA which may interact synergistically. The family is necessary for correct biofilm formation, as null mutants of ymcA and ylbF fail to form pellicles at air-liquid interfaces and grow on solid media as smooth, undifferentiated colonies. During development, YmcA, YlbF and YaaT, family PSPI, pfam04468, interact directly with one another forming a stable ternary complex, in vitro. All three proteins are required for competence, sporulation and the formation of biofilms. The YmcA-YlbF-YaaT complex affects the phosphotransfer between Spo0F and Spo0B, thus accelerating the production of Spo0A~P. The three processes of biofilm formation, mature spore formation and competence all require the active, phosphorylated form of Spo0A, as Spo0A-P.


Pssm-ID: 428784 [Multi-domain]  Cd Length: 103  Bit Score: 37.52  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    334 REVENLIKENSELLDMKNALNIVKND--LINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLK--QKLMEK 409
Cdd:pfam06133    4 RELAKAIKESEEYKRYKEAEEALEADeeAQKLIKEFRKLQEELQEKQMQGEELTEEEKQELQELYEELDQNPlvAEYLEA 83

                   ...
gi 71996943    410 ENE 412
Cdd:pfam06133   84 EQE 86
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
374-460 8.04e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 8.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943    374 LRDENLSR--QMVSEKMQEQiTKHEEEIKTLKQKLMEKENEQEEDDvpmAMRKRFTRSEMQRVLMDRNAYKEKLMELEES 451
Cdd:pfam15709  363 LQQEQLERaeKMREELELEQ-QRRFEEIRLRKQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRKLQELQRK 438

                   ....*....
gi 71996943    452 IKWTEMQRA 460
Cdd:pfam15709  439 KQQEEAERA 447
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
70-416 9.20e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943   70 LVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLE 149
Cdd:COG4372   25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  150 LKAKNATDHASRLEEREVEQKL---EFDRLHERYNTLLRTHVDHMERTKYLMgSEKFELMQNMPLPNMQLRNKMgmaasv 226
Cdd:COG4372  105 SLQEEAEELQEELEELQKERQDleqQRKQLEAQIAELQSEIAEREEELKELE-EQLESLQEELAALEQELQALS------ 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  227 DASSIRGVSDLISAHMTQSTTMDVNLANHITNEDWQDEFSS-DIEPSPRDIPQSSADALTSPITTKEPTPKREAASPKQS 305
Cdd:COG4372  178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEeLLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943  306 EEEEADETTSVDPKENNDLLGADLTGMGREVENLIKENSELLDM-KNALNIVKNDLINQVDELNSENMILRDENLSRQMV 384
Cdd:COG4372  258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLlNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
                        330       340       350
                 ....*....|....*....|....*....|..
gi 71996943  385 SEKMQEQITKHEEEIKTLKQKLMEKENEQEED 416
Cdd:COG4372  338 ELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
84-185 9.73e-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: 9.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996943     84 ERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDtligQNKELDKKIESLESIMRMLELKAKNATDHASRLE 163
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES----RLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                           90       100
                   ....*....|....*....|..
gi 71996943    164 EREVEQKLEFDRLHERYNTLLR 185
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLK 428
 
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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