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Conserved domains on  [gi|1622878982|ref|XP_028692186|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform X5 [Macaca mulatta]

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 ...
 24-178 6.82e-70

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: 230.58  E-value: 6.82e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878982  104 IEFEDSQEQEKKDLQTRVESLESQTRQLElkaknyADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTK 178
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.
 961-1315 7.33e-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: 161.34  E-value: 7.33e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  961 PNEQDLVREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1034
Cdd:pfam19056   80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1035 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1114
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1115 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPLTetnKTSGVPgnr 1194
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVP---RLEGIP--- 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1195 pgsvirvygdensdKVTPGTFIPYcsmahaqlcfHGHRDAVKFFVAVpgqvispqSSSSGTDLTGDKAGPSAQEPgsqtp 1274
Cdd:pfam19056  308 --------------KITGKGMVSL----------NAHCGPVKFLVAA--------SSTLPDLLKRDKEKEESSSA----- 350

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622878982 1275 lksmlviSGGEGYIDfrmgDEGGESELLGEDLPLEPSVTKA 1315
Cdd:pfam19056  351 -------SGSEPKPD----GDSKESLPGLEASAPSPSRKKG 380
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 415-467 1.04e-19

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: 84.28  E-value: 1.04e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622878982  415 MGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQA 467
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAA 53
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
66-363 1.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372     57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  140 DQISRLEEREAELKKEYNALH------QRHTEMIHNYMEHLERTKLHQlsGSDQLESTAHSRIRKERPISLGIFPLPAgD 213
Cdd:COG4372    136 AQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ--ALDELLKEANRNAEKEEELAEAEKLIES-L 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  214 GLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIptdtp 293
Cdd:COG4372    213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA----- 287

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  294 LKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGS 363
Cdd:COG4372    288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
 
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 ...
 24-178 6.82e-70

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: 230.58  E-value: 6.82e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878982  104 IEFEDSQEQEKKDLQTRVESLESQTRQLElkaknyADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTK 178
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 961-1315 7.33e-42

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 161.34  E-value: 7.33e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  961 PNEQDLVREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1034
Cdd:pfam19056   80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1035 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1114
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1115 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPLTetnKTSGVPgnr 1194
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVP---RLEGIP--- 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1195 pgsvirvygdensdKVTPGTFIPYcsmahaqlcfHGHRDAVKFFVAVpgqvispqSSSSGTDLTGDKAGPSAQEPgsqtp 1274
Cdd:pfam19056  308 --------------KITGKGMVSL----------NAHCGPVKFLVAA--------SSTLPDLLKRDKEKEESSSA----- 350

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622878982 1275 lksmlviSGGEGYIDfrmgDEGGESELLGEDLPLEPSVTKA 1315
Cdd:pfam19056  351 -------SGSEPKPD----GDSKESLPGLEASAPSPSRKKG 380
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 415-467 1.04e-19

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: 84.28  E-value: 1.04e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622878982  415 MGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQA 467
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAA 53
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 27-96 9.58e-10

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: 56.45  E-value: 9.58e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445     21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-195 1.67e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717    319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717    393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460

                          170
                   ....*....|....*...
gi 1622878982  178 KLHQLSGSDQLESTAHSR 195
Cdd:COG4717    461 ELEQLEEDGELAELLQEL 478
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 67-176 7.00e-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: 47.32  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622878982  140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523  440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-178 1.94e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918   224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878982  109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918   304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
980-1177 2.78e-04

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  980 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1052
Cdd:COG3292    186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1053 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1125
Cdd:COG3292    263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622878982 1126 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1177
Cdd:COG3292    341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
66-363 1.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372     57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  140 DQISRLEEREAELKKEYNALH------QRHTEMIHNYMEHLERTKLHQlsGSDQLESTAHSRIRKERPISLGIFPLPAgD 213
Cdd:COG4372    136 AQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ--ALDELLKEANRNAEKEEELAEAEKLIES-L 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  214 GLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIptdtp 293
Cdd:COG4372    213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA----- 287

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  294 LKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGS 363
Cdd:COG4372    288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
 
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 ...
 24-178 6.82e-70

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: 230.58  E-value: 6.82e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878982  104 IEFEDSQEQEKKDLQTRVESLESQTRQLElkaknyADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTK 178
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 961-1315 7.33e-42

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 161.34  E-value: 7.33e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  961 PNEQDLVREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1034
Cdd:pfam19056   80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1035 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1114
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1115 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPLTetnKTSGVPgnr 1194
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVP---RLEGIP--- 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1195 pgsvirvygdensdKVTPGTFIPYcsmahaqlcfHGHRDAVKFFVAVpgqvispqSSSSGTDLTGDKAGPSAQEPgsqtp 1274
Cdd:pfam19056  308 --------------KITGKGMVSL----------NAHCGPVKFLVAA--------SSTLPDLLKRDKEKEESSSA----- 350

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622878982 1275 lksmlviSGGEGYIDfrmgDEGGESELLGEDLPLEPSVTKA 1315
Cdd:pfam19056  351 -------SGSEPKPD----GDSKESLPGLEASAPSPSRKKG 380
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 415-467 1.04e-19

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: 84.28  E-value: 1.04e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622878982  415 MGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQA 467
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAA 53
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 27-96 9.58e-10

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: 56.45  E-value: 9.58e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445     21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-195 1.67e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717    319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717    393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460

                          170
                   ....*....|....*...
gi 1622878982  178 KLHQLSGSDQLESTAHSR 195
Cdd:COG4717    461 ELEQLEEDGELAELLQEL 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-162 2.71e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   61 LDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ---TRVESLESQTRQLELKAKN 137
Cdd:COG1196    234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRE 313

                           90       100
                   ....*....|....*....|....*
gi 1622878982  138 YADQISRLEEREAELKKEYNALHQR 162
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEE 338
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 67-176 7.00e-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: 47.32  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622878982  140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523  440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-159 8.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 8.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLESQTRQLELKAKNYADQI 142
Cdd:COG1196    260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                           90
                   ....*....|....*..
gi 1622878982  143 SRLEEREAELKKEYNAL 159
Cdd:COG1196    340 EELEEELEEAEEELEEA 356
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-176 8.75e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   31 IYREFERLIGRYDEevvkelmplVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFED 108
Cdd:COG4913    260 LAERYAAARERLAE---------LEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEA 330

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622878982  109 SQEQ----EKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLER 176
Cdd:COG4913    331 QIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-178 1.94e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918   224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878982  109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918   304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
980-1177 2.78e-04

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  980 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1052
Cdd:COG3292    186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982 1053 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1125
Cdd:COG3292    263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622878982 1126 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1177
Cdd:COG3292    341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-200 2.98e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196    281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622878982  146 EEREAELKKEYNALHQRHTEMIHNYMEHLE--------RTKLHQLSGSDQLESTAHSRIRKER 200
Cdd:COG1196    361 AEAEEALLEAEAELAEAEEELEELAEELLEalraaaelAAQLEELEEAEEALLERLERLEEEL 423
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
59-166 5.32e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   59 ENLDSVFAQDQEHQVELELLRDDNEQLitqYEREKALRKHAEEKFIEFEDSQEqEKKDLQTRVESLESQTRQLELKAKNY 138
Cdd:PRK02224   328 DRLEECRVAAQAHNEEAESLREDADDL---EERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDA 403

                           90       100
                   ....*....|....*....|....*...
gi 1622878982  139 ADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:PRK02224   404 PVDLGNAEDFLEELREERDELREREAEL 431
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
28-166 5.96e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   28 AGSIYREFERLIGRYDEEVVKELM-PLVVAVLENLDsvfAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEF 106
Cdd:COG3206    238 AEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLA---ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622878982  107 EDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLE--EREAELKKE-YNALHQRHTEM 166
Cdd:COG3206    315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElYESLLQRLEEA 377
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-192 7.88e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 7.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQ-----------------EQEKKDLQTRVESLESQT 128
Cdd:COG1196    330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaeeeleelaeelleaLRAAAELAAQLEELEEAE 409

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878982  129 RQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLESTA 192
Cdd:COG1196    410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 65-165 8.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 8.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   65 FAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDL---QTRVESLESQTRQLELKAKNYADQ 141
Cdd:COG1196    231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEER 310

                           90       100
                   ....*....|....*....|....
gi 1622878982  142 ISRLEEREAELKKEYNALHQRHTE 165
Cdd:COG1196    311 RRELEERLEELEEELAELEEELEE 334
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 34-199 1.35e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.92  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   34 EFERLIGRYDEEVvKELMPLvvavLENLDsvfaqDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDS---Q 110
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLAL----LENLE-----LDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYlehA 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  111 EQEKKDLQTRVESLeSQTRQL---EL-KAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYME---HLERTKLHQLS 183
Cdd:pfam06160  304 EEQNKELKEELERV-QQSYTLnenELeRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEileQLEEIEEEQEE 382

                          170
                   ....*....|....*.
gi 1622878982  184 GSDQLEStahsrIRKE 199
Cdd:pfam06160  383 FKESLQS-----LRKD 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 53-174 1.46e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   53 LVVAVLENLDSVFAQDQEHQVELELlrDDNEQLITQYEREKAlrkhaeekfiefedSQEQEKKDLQTRVESLESQTRQLE 132
Cdd:COG4942      5 LLLALLLALAAAAQADAAAEAEAEL--EQLQQEIAELEKELA--------------ALKKEEKALLKQLAALERRIAALA 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622878982  133 LKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHL 174
Cdd:COG4942     69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-177 1.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   32 YREFERLIGRYDEEVVKELMplvvAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAE--EKFIEFEDs 109
Cdd:COG4717     55 ADELFKPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP- 129

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878982  110 QEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAE---LKKEYNALHQRHTEMIHNYMEHLERT 177
Cdd:COG4717    130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElaeLQEELEELLEQLSLATEEELQDLAEE 200
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
66-363 1.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372     57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  140 DQISRLEEREAELKKEYNALH------QRHTEMIHNYMEHLERTKLHQlsGSDQLESTAHSRIRKERPISLGIFPLPAgD 213
Cdd:COG4372    136 AQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ--ALDELLKEANRNAEKEEELAEAEKLIES-L 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  214 GLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIptdtp 293
Cdd:COG4372    213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA----- 287

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  294 LKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGS 363
Cdd:COG4372    288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 50-159 2.23e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   50 LMP------LVVAVLENLDSVFAQDQEHQ-VELELLRDDNEQLITQYEREKA---------LRKHAEEKFIEFEDSQEQE 113
Cdd:PRK05771     1 LAPvrmkkvLIVTLKSYKDEVLEALHELGvVHIEDLKEELSNERLRKLRSLLtklsealdkLRSYLPKLNPLREEKKKVS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1622878982  114 KKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNAL 159
Cdd:PRK05771    81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 55-165 2.51e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.54  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   55 VAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-------YEREkaLRKHAEekfiefeDSQEQEKkdLQTRVESLESQ 127
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIareaqqnYERE--LVLHAE-------DIKALQA--LREELNELKAE 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622878982  128 TRQLELKAKNYADQISRLE----EREAELKKEYNALHQRHTE 165
Cdd:pfam07926   73 IAELKAEAESAKAELEESEesweEQKKELEKELSELEKRIED 114
PRK12704 PRK12704
phosphodiesterase; Provisional
 66-176 2.84e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELlRDDNEQLITQYEREKALRKhaeekfiefEDSQEQEKKdLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:PRK12704    51 AEAIKKEALLEA-KEEIHKLRNEFEKELRERR---------NELQKLEKR-LLQKEENLDRKLELLEKREEELEKKEKEL 119

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622878982  146 EEREAELKKEYNALHQRHTEMIhnymEHLER 176
Cdd:PRK12704   120 EQKQQELEKKEEELEELIEEQL----QELER 146
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 65-182 2.91e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 41.25  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   65 FAQDQEHqVELELLRDDNE--------QLITQYEREKALRKHAEEKFIEFEDSQeQEKKDLQTRVESLESQTRQLELKAK 136
Cdd:COG4026     96 LGHDVEY-VDVELVRKEIKnaiiraglKSLQNIPEYNELREELLELKEKIDEIA-KEKEKLTKENEELESELEELREEYK 173

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1622878982  137 NYADQISRLEEREAELKKEYNALHQRHTEMIHNymEHLERTKLHQL 182
Cdd:COG4026    174 KLREENSILEEEFDNIKSEYSDLKSRFEELLKK--RLLEVFSLEEL 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-200 2.95e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982  113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEST 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452


                   ....*....
gi 1622878982  192 AHSRIRKER 200
Cdd:TIGR02168  453 QEELERLEE 461
Filament pfam00038
Intermediate filament protein;
72-193 3.17e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   72 QVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLesqTRQLELKAKNYADQISRLEE- 147
Cdd:pfam00038   74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKNHEEEVRELQAq 150

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878982  148 -------------REAELKKEYNALHQRHTEMIHNYMEHLE---RTKLHQL-----SGSDQLESTAH 193
Cdd:pfam00038  151 vsdtqvnvemdaaRKLDLTSALAEIRAQYEEIAAKNREEAEewyQSKLEELqqaaaRNGDALRSAKE 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 69-167 4.47e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   69 QEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEER 148
Cdd:COG1196    277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                           90
                   ....*....|....*....
gi 1622878982  149 EAELKKEYNALHQRHTEMI 167
Cdd:COG1196    357 EAELAEAEEALLEAEAELA 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 74-155 4.58e-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: 41.54  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   74 ELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ----------TRVESLESQTRQLELKAKNYADQIS 143
Cdd:TIGR04523  441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkskeKELKKLNEEKKELEEKVKDLTKKIS 520

                           90
                   ....*....|..
gi 1622878982  144 RLEEREAELKKE 155
Cdd:TIGR04523  521 SLKEKIEKLESE 532
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 23-166 6.04e-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: 40.65  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   23 RVSGLAGSIyREFERLIGRYDEEVV------KELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-YEREKAL 95
Cdd:pfam07888   74 QRRELESRV-AELKEELRQSREKHEeleekyKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvLERETEL 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   96 RKHAE--EKFIEFEDSQEQEKKDLQTRVESLESQTRQLEL---KAKNYADQ----ISRLEEREAELKKEYNALHQRHTEM 166
Cdd:pfam07888  153 ERMKEraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKEAEN 232
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 60-166 6.59e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   60 NLDSVFAQDQEHQVELELLRDDNEQLITQYERE---------------KALRKHAEEKFIEFEDSQEQEKKDLQTrVESL 124
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnsesenSEKQRELEEKQNEIEKLKKENQSYKQE-IKNL 389

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622878982  125 ESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:TIGR04523  390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 72-154 6.86e-03

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 38.91  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   72 QVELELLRD-DNEQLITQYE------REK-ALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQIS 143
Cdd:pfam05300   66 KIKEELYKRlEQEQAKVQEElarlaeREReAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLA 145

                           90
                   ....*....|.
gi 1622878982  144 RLEEREAELKK 154
Cdd:pfam05300  146 RLEEKNAEFYK 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-200 7.36e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLElkakNYADQISRL 145
Cdd:COG1196    323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL----EALRAAAEL 398

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622878982  146 EEREAELKKEYNALHQRHTEmihnyMEHLERTKLHQLSGSDQLESTAHSRIRKER 200
Cdd:COG1196    399 AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAA 448
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
56-162 7.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   56 AVLENLDSVFAQDQEHQVELELLRDDNEQLITQYERekaLRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKA 135
Cdd:COG4717    139 AELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                           90       100
                   ....*....|....*....|....*..
gi 1622878982  136 KNYADQISRLEEREAELKKEYNALHQR 162
Cdd:COG4717    216 EEAQEELEELEEELEQLENELEAAALE 242
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 66-155 7.77e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLesqtRQLELKAKNYADQISR- 144
Cdd:pfam13868  238 QQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE----KQIEEREEQRAAEREEe 313

                           90
                   ....*....|.
gi 1622878982  145 LEEREAELKKE 155
Cdd:pfam13868  314 LEEGERLREEE 324
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 58-158 8.86e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 8.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   58 LENLDSVFAQDQEhqvELELLRDDNEQLitqyEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKN 137
Cdd:COG3883    121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                           90       100
                   ....*....|....*....|.
gi 1622878982  138 YADQISRLEEREAELKKEYNA 158
Cdd:COG3883    194 AEAQLAELEAELAAAEAAAAA 214
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 80-189 9.81e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 9.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878982   80 DDNEQLITQYEREKA-LRKHAEEKFIEFEDSQeQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELK----- 153
Cdd:pfam13851   22 RNNLELIKSLKEEIAeLKKKEERNEKLMSEIQ-QENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKvleke 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622878982  154 -------------------KEYNALHQRHTEMIHNYMEH-------LERtKLHQLsgSDQLE 189
Cdd:pfam13851  101 lkdlkwehevleqrfekveRERDELYDKFEAAIQDVQQKtglknllLEK-KLQAL--GETLE 159
 
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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