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Conserved domains on  [gi|187951607|gb|AAI37125|]
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Mitogen-activated protein kinase 8 interacting protein 3 [Homo sapiens]

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 ...
 29-184 8.48e-74

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: 241.75  E-value: 8.48e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187951607   109 IEFEDALEQEKKELQIQVEHYEFQTRQLElkaknyADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKM 184
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 947-1171 8.21e-48

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: 179.06  E-value: 8.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   947 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1024
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  1025 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1104
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187951607  1105 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1171
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 416-484 4.98e-29

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: 110.86  E-value: 4.98e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187951607   416 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 484
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
Trypan_PARP super family cl42451
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 842-956 9.36e-10

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


The actual alignment was detected with superfamily member pfam05887:

Pssm-ID: 368653  Cd Length: 134  Bit Score: 58.26  E-value: 9.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   842 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 918
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 187951607   919 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 956
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 427-553 1.97e-04

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   427 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 503
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187951607   504 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 553
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
 
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 ...
 29-184 8.48e-74

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: 241.75  E-value: 8.48e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187951607   109 IEFEDALEQEKKELQIQVEHYEFQTRQLElkaknyADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKM 184
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 947-1171 8.21e-48

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 179.06  E-value: 8.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   947 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1024
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  1025 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1104
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187951607  1105 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1171
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 416-484 4.98e-29

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: 110.86  E-value: 4.98e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187951607   416 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 484
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 32-103 2.11e-12

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: 64.15  E-value: 2.11e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187951607   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRRQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 842-956 9.36e-10

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 58.26  E-value: 9.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   842 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 918
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 187951607   919 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 956
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-182 5.97e-07

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: 53.87  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRRQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187951607   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-167 4.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 187951607  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1045-1167 5.88e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607 1045 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1117
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 187951607 1118 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 1167
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 6.99e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187951607  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK11633 PRK11633
cell division protein DedD; Provisional
 888-975 7.99e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.38  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  888 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 962
Cdd:PRK11633   64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143

                          90
                  ....*....|...
gi 187951607  963 AGSSAAPTMWLGA 975
Cdd:PRK11633  144 APTGKAYVVQLGA 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 427-553 1.97e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   427 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 503
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187951607   504 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 553
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 442-522 1.04e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  442 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 511
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596

                          90
                  ....*....|.
gi 187951607  512 SDKIPMAQRRR 522
Cdd:PRK00409  597 QKGGYASVKAH 607
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 441-561 1.21e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.29  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   441 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 517
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 187951607   518 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 561
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
427-569 2.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  427 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 503
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187951607  504 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 569
Cdd:COG4372   169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 455-503 3.81e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.39  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187951607  455 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 503
Cdd:COG0711    33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 897-968 4.05e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 41.14  E-value: 4.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187951607  897 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 968
Cdd:NF041121   17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 455-503 4.71e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 4.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187951607  455 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 503
Cdd:cd06503    32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-188 9.61e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 9.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607     86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|....*..
gi 187951607    164 --LHQRHTEMIQTYVEHIERSkMQQVG 188
Cdd:smart00935   83 qdLQKRQQEELQKILDKINKA-IKEVA 108
 
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 ...
 29-184 8.48e-74

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: 241.75  E-value: 8.48e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187951607   109 IEFEDALEQEKKELQIQVEHYEFQTRQLElkaknyADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKM 184
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 947-1171 8.21e-48

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 179.06  E-value: 8.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   947 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1024
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  1025 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1104
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187951607  1105 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1171
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 416-484 4.98e-29

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: 110.86  E-value: 4.98e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187951607   416 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 484
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 32-103 2.11e-12

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: 64.15  E-value: 2.11e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187951607   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRRQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 842-956 9.36e-10

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 58.26  E-value: 9.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   842 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 918
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 187951607   919 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 956
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-182 5.97e-07

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: 53.87  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRRQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187951607   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 39-185 1.70e-05

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: 49.08  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    39 EFERLIHCYDEEVvKELMPLVVNVleNLDSVLSENQEHEVELELLREdneqlltQYEREKALRRQAEEKFIEFEDALEQ- 117
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLALLENL--ELDEAEEALEEIEERIDQLYD-------LLEKEVDAKKYVEKNLPEIEDYLEHa 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187951607   118 --EKKELQIQVEH----YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQ 185
Cdd:pfam06160  304 eeQNKELKEELERvqqsYTLNENELE-RVRGLEKQLEELEKRYDEIVERLEEKEVAYSE-LQEELEEILEQLEE 375
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-167 4.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 187951607  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1045-1167 5.88e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607 1045 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1117
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 187951607 1118 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 1167
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 6.99e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187951607  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK11633 PRK11633
cell division protein DedD; Provisional
 888-975 7.99e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.38  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  888 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 962
Cdd:PRK11633   64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143

                          90
                  ....*....|...
gi 187951607  963 AGSSAAPTMWLGA 975
Cdd:PRK11633  144 APTGKAYVVQLGA 156
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 8.64e-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: 8.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   79 ELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          90       100
                  ....*....|....*....|....*..
gi 187951607  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEA 402
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-182 1.00e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   48 DEEVVKELMPLVVNVLENLDSVLSE--NQEHEVELELLREDNEQLLTQY--EREKALRRQAEEKfiEFEDALEQEKKELQ 123
Cdd:COG4717   331 PPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQA--EEYQELKEELEELE 408

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187951607  124 IQVE-HYEFQTRQLE-LKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERS 182
Cdd:COG4717   409 EQLEeLLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAE-LEAELEQLEED 468
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-160 1.01e-04

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: 46.07  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    70 LSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE----QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312

                           90
                   ....*....|..
gi 187951607   150 -LEERESEMKKE 160
Cdd:pfam13868  313 eLEEGERLREEE 324
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 64-160 1.21e-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: 46.55  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKALRRQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 187951607   123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523  492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
Filament pfam00038
Intermediate filament protein;
66-185 1.35e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.68  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038   63 LDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKN 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 187951607   143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038  140 HEEEVRELQAQVSdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-186 1.64e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4372    25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 187951607  138 LKAKNYADQISRLEEREsemkKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   105 SLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 427-553 1.97e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   427 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 503
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187951607   504 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 553
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
PRK12495 PRK12495
hypothetical protein; Provisional
 864-965 2.74e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 44.09  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  864 SRGDTPVLDKGQG-EVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATL-------RPGPLTEHVFTDPAPTPSSGP 935
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTsatdeaaTDPPATAAARDGPTPDPTAQP 148

                          90       100       110
                  ....*....|....*....|....*....|.
gi 187951607  936 -QPGSENGPEPDSSSTRPEPEPSGDPTGAGS 965
Cdd:PRK12495  149 aTPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 89-204 3.31e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    89 QLLTQYEREKAL-RRQAEEKFIEFE-DALEQEKKELQIQVEHY----EFQT-RQLEL--KAKNYADQISRLEERESEM-- 157
Cdd:pfam17380  273 QLLHIVQHQKAVsERQQQEKFEKMEqERLRQEKEEKAREVERRrkleEAEKaRQAEMdrQAAIYAEQERMAMERERELer 352

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 187951607   158 ------KKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKER 204
Cdd:pfam17380  353 irqeerKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK 405
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-186 3.50e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   62 VLENLDSVLSENQEHEVELELLRED----NEQLLTQYEREKALRRQAEEKFIEFEDA------LEQEKKELQIQVEHYEF 131
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEEleqaRSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187951607  132 QTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ 183
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 863-970 3.63e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  863 SSRGDTPVLDKGQGEVATIAngkvnpSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENG 942
Cdd:PRK07764  400 SAAAAAPAAAPAPAAAAPAA------AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA 473

                          90       100
                  ....*....|....*....|....*...
gi 187951607  943 PEPdssSTRPEPEPSGDPTGAGSSAAPT 970
Cdd:PRK07764  474 PEP---TAAPAPAPPAAPAPAAAPAAPA 498
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 66-185 3.66e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 44.17  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    66 LDSVLSENQEH--EVELELLREDNEQLLTQYEREKALRRQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKa 140
Cdd:pfam09728  172 LQQATEEEEKKaqEKEVAKARELKAQVQTLSETEKELREQLNlyvEKFEEFQDTLNKSNEV---------FTTFKKEME- 241

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 187951607   141 kNYADQISRLEERESEMKKEYNALHQRHTEMI---QTYVEHIERSKMQ 185
Cdd:pfam09728  242 -KMSKKIKKLEKENLTWKRKWEKSNKALLEMAeerQKLKEELEKLQKK 288
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 60-167 3.95e-04

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: 41.86  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    60 VNVLENLDSVLSENQEHEVELELLREDNE---QLLTQ----YERE--------KALRR------QAEEKFIEFEDALEQE 118
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaEIAREaqqnYERElvlhaediKALQAlreelnELKAEIAELKAEAESA 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 187951607   119 KKELQIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQR 167
Cdd:pfam07926   84 KAELEESEESWEEQKKELE-------KELSELEKRIEDLNEQNKLLHDQ 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-186 3.99e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 187951607  141 KNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-170 4.42e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLELKAK- 141
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQl 402

                          90       100       110
                  ....*....|....*....|....*....|
gi 187951607  142 -NYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196   403 eELEEAEEALLERLERLEEELEELEEALAE 432
PRK12704 PRK12704
phosphodiesterase; Provisional
 72-152 5.87e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   72 ENQEHEVELELlREDNEQLLTQYEREKALRR----QAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704   52 EAIKKEALLEA-KEEIHKLRNEFEKELRERRnelqKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130

                          90
                  ....*....|....*.
gi 187951607  141 KNY----ADQISRLEE 152
Cdd:PRK12704  131 EELeeliEEQLQELER 146
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 858-972 6.21e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  858 PRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQP 937
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARE 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 187951607  938 GSengPEPDSSSTRPEPEPSGDPTGAGSSAAPTMW 972
Cdd:PHA03307  104 GS---PTPPGPSSPDPPPPTPPPASPPPSPAPDLS 135
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-183 6.84e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   74 QEHEVELELLREDNEQLLTQYEREKALRRQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 187951607  152 ERE---SEMKKEYNALHQRHT--EMIQTYVEHIERSK 183
Cdd:PRK03918  342 ELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-183 7.31e-04

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: 43.37  E-value: 7.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    72 ENQEHEVELELLREDNEQL----LTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQV--EHYEFQTRQLELKAKNyad 145
Cdd:pfam13868   70 ERKRYRQELEEQIEEREQKrqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE--- 146

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 187951607   146 qisRLEERESEMK-KEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  147 ---KEEEREEDERiLEYLKEKAEREEEREAEREEIEEEK 182
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 67-194 8.40e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKALRRQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269   169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 187951607  145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVGGNSQTE 194
Cdd:cd16269   237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEGFKEQAE 281
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 71-202 9.68e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    71 SENQEHEVELELLREDNEQLLTQYERekalRRQAEEkfiEFEDALEQEKKELQIQVEHYEFQ------TRQ--------L 136
Cdd:pfam01576   57 AEAEEMRARLAARKQELEEILHELES----RLEEEE---ERSQQLQNEKKKMQQHIQDLEEQldeeeaARQklqlekvtT 129

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187951607   137 ELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQ--TESSLPGRRK 202
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeaMISDLEERLK 197
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 442-522 1.04e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  442 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 511
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596

                          90
                  ....*....|.
gi 187951607  512 SDKIPMAQRRR 522
Cdd:PRK00409  597 QKGGYASVKAH 607
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 39-160 1.08e-03

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.22  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   39 EFERLIHCYDEEVVKELMPLVVNVLENLdsvLSENQEhevelelLREDNEQL---LTQY-EREKALRR---QAEEkfiEF 111
Cdd:COG3599    12 EFKKGFRGYDEDEVDEFLDEVAEDYERL---IRENKE-------LKEKLEELeeeLEEYrELEETLQKtlvVAQE---TA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 187951607  112 EDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEresEMKKE 160
Cdd:COG3599    79 EEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIE---ELKRQ 124
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-186 1.21e-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: 42.60  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    72 ENQEHEVElELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQeKKELQIQVEHYEfQTRQLE----LKAKNYADQI 147
Cdd:pfam13868   30 EKKRIKAE-EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIEERE-QKRQEEyeekLQEREQMDEI 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 187951607   148 SRLEERESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  107 VERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEK 147
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 441-561 1.21e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.29  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   441 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 517
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 187951607   518 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 561
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-179 1.24e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL----KAKNYADQISRLEERESEMKKEY 161
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereeKEQELQKKEQELQQLQQKAQQEL 85

                           90
                   ....*....|....*...
gi 187951607   162 NALHQRHTEMIQTYVEHI 179
Cdd:pfam03938   86 QKKQQELLQPIQDKINKA 103
GreA_GreB_N pfam03449
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
 460-487 1.28e-03

Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.


Pssm-ID: 460920 [Multi-domain]  Cd Length: 71  Bit Score: 38.51  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....*...
gi 187951607   460 GELEAAKQAKVKLENRIKELEEELKRVK 487
Cdd:pfam03449   43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-163 1.44e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883   121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                          90       100
                  ....*....|....*....|.
gi 187951607  143 YADQISRLEERESEMKKEYNA 163
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAA 214
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 63-168 1.44e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 41.35  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRR----QAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL 138
Cdd:pfam06785   85 FKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQiqlqQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRS 164

                           90       100       110
                   ....*....|....*....|....*....|
gi 187951607   139 KAKNYADQISRLEERESEMKKEYNALHQRH 168
Cdd:pfam06785  165 VLEKRQDQIENLESKVRDLNYEIKTLLQLA 194
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 76-171 1.54e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 40.24  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    76 HEVELELLREDNEQLLTQYEREKALRRQAEEKFI---------EFEDALEQEKKELQIQVEhyefqtrqlelkaknyadQ 146
Cdd:pfam12474   23 YEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIraeqkkrlkMFRESLKQEKKELKQEVE------------------K 84

                           90       100
                   ....*....|....*....|....*.
gi 187951607   147 ISRLEERESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474   85 LPKFQRKEAKrQRKEELELEQKHEEL 110
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 888-970 1.66e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  888 PSQSTEEATEATEVPDPGPSEPETATLRPGPltehVFTDPAPTPSSGPQP--GSENGPEPDSSSTRPEPEPSGDPTGAGS 965
Cdd:PRK07764  396 AAAPSAAAAAPAAAPAPAAAAPAAAAAPAPA----AAPQPAPAPAPAPAPpsPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471


                  ....*
gi 187951607  966 SAAPT 970
Cdd:PRK07764  472 AAPEP 476
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 39-203 2.01e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.64  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   39 EFERLIHCYDEEVVK---ELMPLVVNVLENLDSVLS--ENQEHEVELELLREDNEQLLTQYEREK----ALRRQAEEKFI 109
Cdd:COG5185   326 ELEESKRETETGIQNltaEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELDSFKDTIESTKesldEIPQNQRGYAQ 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  110 EFEDALEQEKKELQIQVEHY----EFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQ 185
Cdd:COG5185   406 EILATLEDTLKAADRQIEELqrqiEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNE 485

                         170
                  ....*....|....*...
gi 187951607  186 QVggnSQTESSLPGRRKE 203
Cdd:COG5185   486 EL---TQIESRVSTLKAT 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 426-572 2.01e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   426 ENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVS 505
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187951607   506 SYlctesdkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASREHPSVQEKKKSTI 572
Cdd:TIGR02169  466 KY----------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE--ERVRGGRAVEEVLKASI 520
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-166 2.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALE-----QEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELE 152

                          90       100
                  ....*....|....*....|....*....
gi 187951607  138 LKAKNYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEE 181
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-186 2.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEkfiefedaLEQEKKELQIQVEHYEFQTRQLELKA-K 141
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE--------LEAELAELQEELEELLEQLSLATEEElQ 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 187951607  142 NYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQQ 186
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAA 239
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 442-489 2.12e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 39.50  E-value: 2.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 187951607   442 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSE 489
Cdd:pfam17675   44 EELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEE 91
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 63-186 2.16e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    63 LENLDSVLS----------------ENQEHEVElELLREDNEQLLT------QYEREKA-LRRQAEEKfiefedalEQEK 119
Cdd:pfam01576  442 LESVSSLLNeaegkniklskdvsslESQLQDTQ-ELLQEETRQKLNlstrlrQLEDERNsLQEQLEEE--------EEAK 512

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187951607   120 KELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ 186
Cdd:pfam01576  513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY-DKLEKTKnrLQQ 580
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 53-179 2.16e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 40.54  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   53 KELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQ--YEREKALR--RQAEEKFIefEDALEQEKKELQIQVEH 128
Cdd:PRK14471   31 KPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEarAERDAILKeaREIKEKMI--ADAKEEAQVEGDKMIEQ 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 187951607  129 YEfQTRQLELKA-----KNYADQISrLEERESEMKKEYNALHQRHtEMIQTYVEHI 179
Cdd:PRK14471  109 AK-ASIESEKNAamaeiKNQVANLS-VEIAEKVLRKELSNKEKQH-KLVEKMLGDV 161
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 63-187 2.17e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKALRRQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778  258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187951607  129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778  338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
427-569 2.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  427 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 503
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187951607  504 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 569
Cdd:COG4372   169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 50-163 2.30e-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: 42.06  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   50 EVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhy 129
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-- 216

                          90       100       110
                  ....*....|....*....|....*....|....
gi 187951607  130 efqtrQLELKAKNYADQISRLEERESEMKKEYNA 163
Cdd:COG4942   217 -----ELQQEAEELEALIARLEAEAAAAAERTPA 245
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 74-183 2.50e-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: 41.83  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    74 QEHEVELELLREDNEQLL----TQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868   87 QKRQEEYEEKLQEREQMDeiveRIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166

                           90       100       110
                   ....*....|....*....|....*....|....
gi 187951607   150 LEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 103-186 2.73e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   103 QAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALHQRHTEM--IQTYVEH 178
Cdd:pfam10368   15 ELEKPFEEQQEPLvELEKKEQELYEEIIELGMDEFD-EIKKLSDEaLENVEEREELLEKEKESIEEAKEEFkkIKEIIEE 93


                   ....*...
gi 187951607   179 IERSKMQQ 186
Cdd:pfam10368   94 IEDEELKK 101
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 74-164 2.73e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   74 QEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELqiqvehyefqtRQLELKAKNYADQISRLEER 153
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-----------KRLELEIEEVEARIKKYEEQ 81

                          90
                  ....*....|...
gi 187951607  154 ESEMK--KEYNAL 164
Cdd:COG1579    82 LGNVRnnKEYEAL 94
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 446-570 3.22e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   446 AKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRV--KSEAIIARREP--------KEEAEDVSSYLCTESDKI 515
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrKIGEIEKEIEQleqeeeklKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 187951607   516 PMAQRrrftrvEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 570
Cdd:TIGR02169  754 ENVKS------ELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 64-165 3.31e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQY--------EREKALRRQAEEkfiEFEDALEQEKKE------- 121
Cdd:PRK00409  516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELeekkeklqEEEDKLLEEAEK---EAQQAIKEAKKEadeiike 592

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 187951607  122 --LQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409  593 lrQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 73-186 3.34e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 41.86  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    73 NQEHEVELELLREDNEQLltqyEREKALRRqaeekfiefEDALEQEKKELQIQVEHyefqtrqlELKAKNYADQISRLEE 152
Cdd:pfam15818  273 NTEMEAELKALKENNQTL----ERDNELQR---------EKVKENEEKFLNLQNEH--------EKALGTWKKHVEELNG 331

                           90       100       110
                   ....*....|....*....|....*....|....
gi 187951607   153 RESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:pfam15818  332 EINEIKNELSSLKETHIKLQEHYNKLCNQKKFEE 365
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-171 3.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   72 ENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADqISRLE 151
Cdd:COG1196   688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELE 766

                          90       100       110
                  ....*....|....*....|....*....|....
gi 187951607  152 ERESEMKK--------------EYNALHQRHTEM 171
Cdd:COG1196   767 RELERLEReiealgpvnllaieEYEELEERYDFL 800
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 455-503 3.81e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.39  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187951607  455 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 503
Cdd:COG0711    33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
442-560 3.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  442 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSylctesdkipmaqrr 521
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE--------------- 112

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 187951607  522 rfTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 560
Cdd:COG4372   113 --LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 380-571 3.85e-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: 41.58  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   380 DSLYHELSTAGSEVIGDVDEGADLLGEFS-VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSG---EQ 455
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   456 EVLRGELEA----AKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSylcTESDKIPMAQRRRFTRVEMARV 531
Cdd:TIGR02168  781 EAEIEELEAqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESL 857

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 187951607   532 LMERNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 571
Cdd:TIGR02168  858 AAEIEELEELIEELESELeALLNERASLEEALALLRSELEE 898
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 59-174 3.99e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   59 VVNVLENLDSVLSENQEHEVELELLRE----DNEQL--------LTQYERE----KALRRQAEEKFIEFEDALEQEKKEL 122
Cdd:COG1579    47 LEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLgnvrnnkeYEALQKEieslKRRISDLEDEILELMERIEELEEEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 187951607  123 QiQVEhyefqtRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:COG1579   127 A-ELE------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 897-968 4.05e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 41.14  E-value: 4.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187951607  897 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 968
Cdd:NF041121   17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 72-170 4.09e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    72 ENQEHEVELELLRED----NEQLLTQYEREKAL---RRQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKAK 141
Cdd:pfam20492    7 EKQELEERLKQYEEEtkkaQEELEESEETAEELeeeRRQAEEEAERLEqkrQEAEEEKERLEESAEMEAEEKEQLEAELA 86

                           90       100       110
                   ....*....|....*....|....*....|....
gi 187951607   142 NYADQISRLEE----RESEMKK-EYNALHQRHTE 170
Cdd:pfam20492   87 EAQEEIARLEEeverKEEEARRlQEELEEAREEE 120
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
442-502 4.38e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 4.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187951607  442 NDLIAKVDQLSGEQEVLRGELEaakqakvKLENRIKELEEELKRVKSEaiiARREPKEEAE 502
Cdd:COG2433   416 RRLEEQVERLEAEVEELEAELE-------EKDERIERLERELSEARSE---ERREIRKDRE 466
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 455-503 4.71e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 4.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187951607  455 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 503
Cdd:cd06503    32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 79-159 5.30e-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: 39.29  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    79 ELELLREDNEQLLTQYEREKAL------------RRQAEEK----FIEFEDALEQEKKelqiQVEHY--EFQTRQLELKA 140
Cdd:pfam05300   60 EEELRKKIKEELYKRLEQEQAKvqeelarlaereREAAQESltraILRERASTEDERL----KAQQLakQLEEKEAELKK 135

                           90       100
                   ....*....|....*....|.
gi 187951607   141 KN--YADQISRLEERESEMKK 159
Cdd:pfam05300  136 QDafYKEQLARLEEKNAEFYK 156
PRK12704 PRK12704
phosphodiesterase; Provisional
 74-173 5.52e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   74 QEHEVELELLREdnEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEER 153
Cdd:PRK12704   45 EEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                          90       100
                  ....*....|....*....|
gi 187951607  154 ESEMKKEYNALHQRHTEMIQ 173
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQ 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-181 5.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 187951607  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
Filament pfam00038
Intermediate filament protein;
410-560 5.83e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 40.29  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   410 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRV 486
Cdd:pfam00038   60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   487 KSEAIiarREPKEEAEDVSSYLctESDKIPmaqrrrftRVEMARVLME-RNQYKE---------------RLMELQEAV- 549
Cdd:pfam00038  140 HEEEV---RELQAQVSDTQVNV--EMDAAR--------KLDLTSALAEiRAQYEEiaaknreeaeewyqsKLEELQQAAa 206

                          170
                   ....*....|.
gi 187951607   550 RWTEMIRASRE 560
Cdd:pfam00038  207 RNGDALRSAKE 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-181 6.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   63 LENLDSVLSENQEhevELELLREDNEQLLTQYEREKALRRQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   276 LEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEE 348

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 187951607  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-183 7.39e-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: 40.81  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    33 AGSIYREFERLIHCYDEEVVkELMPLVVNVLENLDSVLSENQEH-------EVELELLREDNEQLLTQYEREKALRRQAE 105
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALaneisrlEQQKQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   106 EKFIEFED---ALEQEKKELQIQVE-------HYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRhtemIQTY 175
Cdd:TIGR02168  330 SKLDELAEelaELEEKLEELKEELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERL 405


                   ....*...
gi 187951607   176 VEHIERSK 183
Cdd:TIGR02168  406 EARLERLE 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-181 7.40e-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: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFED---ALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEELEEAEEELEEAEAELAEAEEAL 367

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 187951607  141 KNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIER 181
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEE 407
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 428-549 7.69e-03

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


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 37.76  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   428 SQLLETKNALNVVKNDLIAKVDQLSgEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAiiarREPKEEAEDVSSY 507
Cdd:pfam04871    8 SEASSLKNENTELKAELQELSKQYN-SLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKE----KEKQSELDDLLLL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 187951607   508 LCTESDKipmaqrrrftrvemarvlmeRNQYKERLMELQEAV 549
Cdd:pfam04871   83 LGDLEEK--------------------VEKYKARLKELGEEV 104
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-186 7.91e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   65 NLDSVLSENQEHEVELELLREDN---EQLLTQYEREKALRRQAEEKFIEFEDALEQEKKEL-QIQVEHYEFQTRQLELKA 140
Cdd:COG4913   662 DVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAED 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 187951607  141 KNYADQISRLEER---------ESEMKKEYNALHQRHTEMIQTYVEHIERsKMQQ 186
Cdd:COG4913   742 LARLELRALLEERfaaalgdavERELRENLEERIDALRARLNRAEEELER-AMRA 795
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 73-186 8.16e-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: 39.90  E-value: 8.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607    73 NQEH----EVELELLREDNEQLLtQYEREKALR---------RQAEEKFIEFEDALEQEKKELQIQVEHYefqtrqlELK 139
Cdd:pfam13868  136 NEEQaewkELEKEEEREEDERIL-EYLKEKAEReeereaereEIEEEKEREIARLRAQQEKAQDEKAERD-------ELR 207

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 187951607   140 AKNYADQISRlEERESEMKKEYNALHQRHtEMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  208 AKLYQEEQER-KERQKEREEAEKKARQRQ-ELQQAREEQIELKERRL 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-166 8.19e-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: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   72 ENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKEL--------QIQVEHYEFQTRQLEL--KAK 141
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaeaelaEAEEELEELAEELLEAlrAAA 396

                          90       100
                  ....*....|....*....|....*
gi 187951607  142 NYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 423-548 8.19e-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: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607  423 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARrepkeeae 502
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LAR-------- 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 187951607  503 dvssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 548
Cdd:COG1196   300 -------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-188 9.61e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 9.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607     86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|....*..
gi 187951607    164 --LHQRHTEMIQTYVEHIERSkMQQVG 188
Cdd:smart00935   83 qdLQKRQQEELQKILDKINKA-IKEVA 108
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-181 9.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951607   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE-DALEQEKKELQIQVEHYEFQTRQL 136
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERERRRARLEALLAAL 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 187951607  137 ELK----AKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   372 GLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
 434-500 9.99e-03

Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.


Pssm-ID: 463241  Cd Length: 134  Bit Score: 37.96  E-value: 9.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187951607   434 KNALNVVKNDLIAKVDQLsgeqEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREpKEE 500
Cdd:pfam11221   59 EATQRELARDLILKAQQI----EYLIDSLPGIGVSEEEQLQRIKELEEELREAEEERQEAVKE-KEE 120
 
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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