NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462548062|ref|XP_054235839|]
View 

C-Jun-amino-terminal kinase-interacting protein 3 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 7.90e-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: 7.90e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548062  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.
956-1180 9.19e-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: 178.67  E-value: 9.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  956 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1033
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062 1034 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1113
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548062 1114 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1180
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
425-493 4.08e-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: 4.08e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548062  425 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 493
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
Trypan_PARP super family cl42451
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
851-965 9.52e-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: 9.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  851 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 927
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462548062  928 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 965
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
436-562 1.95e-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: 46.20  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 512
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  513 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 562
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
63-310 4.73e-04

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 4.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883    121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRSPRQSWRKSRKERPTSLNVF 220
Cdd:COG3883    194 AEAQLAELEAELAAAEAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  221 PLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNES 300
Cdd:COG3883    274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353
                          250
                   ....*....|
gi 2462548062  301 LQPLGDYGVG 310
Cdd:COG3883    354 GGGGSSSGGG 363
 
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 7.90e-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: 7.90e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548062  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.
956-1180 9.19e-48

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 178.67  E-value: 9.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  956 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1033
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062 1034 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1113
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548062 1114 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1180
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
425-493 4.08e-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: 4.08e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548062  425 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 493
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 2.00e-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: 2.00e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548062   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRRQ 103
Cdd:cd14445     21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
851-965 9.52e-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: 9.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  851 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 927
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462548062  928 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 965
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 6.12e-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: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRRQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548062  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 4.60e-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: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196    234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313
                           90       100
                   ....*....|....*....|....*
gi 2462548062  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEE 338
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1054-1176 5.93e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062 1054 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1126
Cdd:COG3292    265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462548062 1127 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 1176
Cdd:COG3292    343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 7.05e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 7.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIE 110
Cdd:PRK03918   167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462548062  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918   247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK11633 PRK11633
cell division protein DedD; Provisional
897-984 8.12e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.38  E-value: 8.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  897 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 971
Cdd:PRK11633    64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143
                           90
                   ....*....|...
gi 2462548062  972 AGSSAAPTMWLGA 984
Cdd:PRK11633   144 APTGKAYVVQLGA 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
436-562 1.95e-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: 46.20  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 512
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  513 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 562
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
63-310 4.73e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 4.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883    121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRSPRQSWRKSRKERPTSLNVF 220
Cdd:COG3883    194 AEAQLAELEAELAAAEAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  221 PLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNES 300
Cdd:COG3883    274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353
                          250
                   ....*....|
gi 2462548062  301 LQPLGDYGVG 310
Cdd:COG3883    354 GGGGSSSGGG 363
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
451-531 1.03e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  451 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 520
Cdd:PRK00409   519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596
                           90
                   ....*....|.
gi 2462548062  521 SDKIPMAQRRR 531
Cdd:PRK00409   597 QKGGYASVKAH 607
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
450-570 1.29e-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: 39.90  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  450 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 526
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462548062  527 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 570
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
436-578 2.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 512
Cdd:COG4372     93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548062  513 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 578
Cdd:COG4372    169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
464-512 3.76e-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: 3.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  464 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 512
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 ...
906-977 4.33e-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: 4.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548062  906 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 977
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 ...
464-512 4.74e-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: 4.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  464 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 512
Cdd:cd06503     32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
86-188 8.97e-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: 8.97e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062    86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82
                            90       100
                    ....*....|....*....|....*..
gi 2462548062   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 7.90e-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: 7.90e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548062  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.
956-1180 9.19e-48

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 178.67  E-value: 9.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  956 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1033
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062 1034 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1113
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548062 1114 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1180
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
425-493 4.08e-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: 4.08e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548062  425 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 493
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 2.00e-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: 2.00e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548062   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRRQ 103
Cdd:cd14445     21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
851-965 9.52e-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: 9.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  851 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 927
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462548062  928 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 965
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 6.12e-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: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRRQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548062  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 1.61e-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: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   39 EFERLIHCYDEEVvKELMPLVVNVleNLDSVLSENQEHEVELELLREdneqlltQYEREKALRRQAEEKFIEFEDALEQ- 117
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLALLENL--ELDEAEEALEEIEERIDQLYD-------LLEKEVDAKKYVEKNLPEIEDYLEHa 303
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462548062  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 4.60e-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: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196    234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313
                           90       100
                   ....*....|....*....|....*
gi 2462548062  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEE 338
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1054-1176 5.93e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062 1054 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1126
Cdd:COG3292    265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462548062 1127 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 1176
Cdd:COG3292    343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 7.05e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 7.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIE 110
Cdd:PRK03918   167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462548062  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918   247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK11633 PRK11633
cell division protein DedD; Provisional
897-984 8.12e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.38  E-value: 8.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  897 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 971
Cdd:PRK11633    64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143
                           90
                   ....*....|...
gi 2462548062  972 AGSSAAPTMWLGA 984
Cdd:PRK11633   144 APTGKAYVVQLGA 156
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 8.71e-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: 8.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   79 ELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913    296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
                           90       100
                   ....*....|....*....|....*..
gi 2462548062  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEA 402
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-182 1.02e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   48 DEEVVKELMPLVVNVLENLDSVLSE--NQEHEVELELLREDNEQLLTQY--EREKALRRQAEEKfiEFEDALEQEKKELQ 123
Cdd:COG4717    331 PPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQA--EEYQELKEELEELE 408
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548062  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 1.04e-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: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   70 LSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE----QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312
                           90
                   ....*....|..
gi 2462548062  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 1.23e-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: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKALRRQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462548062  123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523  492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
Filament pfam00038
Intermediate filament protein;
66-185 1.33e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.68  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038   63 LDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKN 139
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038  140 HEEEVRELQAQVSdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-186 1.65e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4372     25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462548062  138 LKAKNYADQISRLEEREsemkKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372    105 SLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAERE 149
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
39-239 1.67e-04

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: 46.10  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   39 EFERLIHCYDEEVVK---ELMPLVVNVLENLDSVLS--ENQEHEVELELLREDNEQLLTQYEREK----ALRRQAEEKFI 109
Cdd:COG5185    326 ELEESKRETETGIQNltaEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELDSFKDTIESTKesldEIPQNQRGYAQ 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  110 EFEDALEQEKKELQIQVEHY----EFQTRQLELKAKNYADQISRLEERESEMKKEYNA-LHQRHTEMIQTYVEHIERSKM 184
Cdd:COG5185    406 EILATLEDTLKAADRQIEELqrqiEQATSSNEEVSKLLNELISELNKVMREADEESQSrLEEAYDEINRSVRSKKEDLNE 485
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  185 ------QQVGGNSQTESSLPGRSPRQ--SWRKSRKERPTSLNVFPLADGTVRAQIGGKLVPAG 239
Cdd:COG5185    486 eltqieSRVSTLKATLEKLRAKLERQleGVRSKLDQVAESLKDFMRARGYAHILALENLIPAS 548
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
436-562 1.95e-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: 46.20  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 512
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  513 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 562
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
PRK12495 PRK12495
hypothetical protein; Provisional
873-974 2.84e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 44.09  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  873 SRGDTPVLDKGQG-EVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATL-------RPGPLTEHVFTDPAPTPSSGP 944
Cdd:PRK12495    69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTsatdeaaTDPPATAAARDGPTPDPTAQP 148
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462548062  945 -QPGSENGPEPDSSSTRPEPEPSGDPTGAGS 974
Cdd:PRK12495   149 aTPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-186 3.52e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   62 VLENLDSVLSENQEHEVELELLRED----NEQLLTQYEREKALRRQAEEKFIEFEDA------LEQEKKELQIQVEHYEF 131
Cdd:COG4372     43 LQEELEQLREELEQAREELEQLEEEleqaRSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQK 122
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548062  132 QTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372    123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ 183
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
872-979 3.72e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  872 SSRGDTPVLDKGQGEVATIAngkvnpSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENG 951
Cdd:PRK07764   400 SAAAAAPAAAPAPAAAAPAA------AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA 473
                           90       100
                   ....*....|....*....|....*...
gi 2462548062  952 PEPdssSTRPEPEPSGDPTGAGSSAAPT 979
Cdd:PRK07764   474 PEP---TAAPAPAPPAAPAPAAAPAAPA 498
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
66-185 3.75e-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: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   66 LDSVLSENQEH--EVELELLREDNEQLLTQYEREKALRRQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKa 140
Cdd:pfam09728  172 LQQATEEEEKKaqEKEVAKARELKAQVQTLSETEKELREQLNlyvEKFEEFQDTLNKSNEV---------FTTFKKEME- 241
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462548062  141 kNYADQISRLEERESEMKKEYNALHQRHTEMI---QTYVEHIERSKMQ 185
Cdd:pfam09728  242 -KMSKKIKKLEKENLTWKRKWEKSNKALLEMAeerQKLKEELEKLQKK 288
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-186 3.85e-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: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196    253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEEL 332
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462548062  141 KNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG1196    333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
35-217 3.86e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   35 SIYREFERLIHCYDEevVKELMPLVVNVLENL-----------DSVLSENQEHEVELELlrEDNEQLLTQYEREKALRRQ 103
Cdd:TIGR00618  567 EIQQSFSILTQCDNR--SKEDIPNLQNITVRLqdlteklseaeDMLACEQHALLRKLQP--EQDLQDVRLHLQQCSQELA 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  104 AEEKfiefedALEQEKKEL-QIQVEHYEFQTRQLELKAKnyadQISRLEERESEMKKEYNA-----LHQRHTEM--IQTY 175
Cdd:TIGR00618  643 LKLT------ALHALQLTLtQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTywkemLAQCQTLLreLETH 712
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462548062  176 VEHIERSKMQQVGGNSQTESSLPGR--SPRQSWRKSRKERPTSL 217
Cdd:TIGR00618  713 IEEYDREFNEIENASSSLGSDLAARedALNQSLKELMHQARTVL 756
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
60-167 3.97e-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: 3.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   60 VNVLENLDSVLSENQEHEVELELLREDNE---QLLTQ----YERE--------KALRR------QAEEKFIEFEDALEQE 118
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaEIAREaqqnYERElvlhaediKALQAlreelnELKAEIAELKAEAESA 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462548062  119 KKELQIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQR 167
Cdd:pfam07926   84 KAELEESEESWEEQKKELE-------KELSELEKRIEDLNEQNKLLHDQ 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-170 4.41e-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: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLELKAK- 141
Cdd:COG1196    323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQl 402
                           90       100       110
                   ....*....|....*....|....*....|
gi 2462548062  142 -NYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196    403 eELEEAEEALLERLERLEEELEELEEALAE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
63-310 4.73e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 4.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883    121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRSPRQSWRKSRKERPTSLNVF 220
Cdd:COG3883    194 AEAQLAELEAELAAAEAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  221 PLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNES 300
Cdd:COG3883    274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353
                          250
                   ....*....|
gi 2462548062  301 LQPLGDYGVG 310
Cdd:COG3883    354 GGGGSSSGGG 363
PRK12704 PRK12704
phosphodiesterase; Provisional
72-152 5.67e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 5.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   72 ENQEHEVELELlREDNEQLLTQYEREKALRR----QAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704    52 EAIKKEALLEA-KEEIHKLRNEFEKELRERRnelqKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130
                           90
                   ....*....|....*.
gi 2462548062  141 KNY----ADQISRLEE 152
Cdd:PRK12704   131 EELeeliEEQLQELER 146
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
867-981 6.76e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 6.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  867 PRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQP 946
Cdd:PHA03307    24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARE 103
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462548062  947 GSengPEPDSSSTRPEPEPSGDPTGAGSSAAPTMW 981
Cdd:PHA03307   104 GS---PTPPGPSSPDPPPPTPPPASPPPSPAPDLS 135
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-183 6.89e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   74 QEHEVELELLREDNEQLLTQYEREKALRRQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918   262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462548062  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 7.69e-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: 7.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   72 ENQEHEVELELLREDNEQL----LTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQV--EHYEFQTRQLELKAKNyad 145
Cdd:pfam13868   70 ERKRYRQELEEQIEEREQKrqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE--- 146
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462548062  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 8.24e-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: 8.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKALRRQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269    169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462548062  145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVGGNSQTE 194
Cdd:cd16269    237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEGFKEQAE 281
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
451-531 1.03e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  451 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 520
Cdd:PRK00409   519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596
                           90
                   ....*....|.
gi 2462548062  521 SDKIPMAQRRR 531
Cdd:PRK00409   597 QKGGYASVKAH 607
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
39-160 1.12e-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: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   39 EFERLIHCYDEEVVKELMPLVVNVLENLdsvLSENQEhevelelLREDNEQL---LTQY-EREKALRR---QAEEkfiEF 111
Cdd:COG3599     12 EFKKGFRGYDEDEVDEFLDEVAEDYERL---IRENKE-------LKEKLEELeeeLEEYrELEETLQKtlvVAQE---TA 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462548062  112 EDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEresEMKKE 160
Cdd:COG3599     79 EEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIE---ELKRQ 124
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
86-179 1.22e-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: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL----KAKNYADQISRLEERESEMKKEY 161
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereeKEQELQKKEQELQQLQQKAQQEL 85
                           90
                   ....*....|....*...
gi 2462548062  162 NALHQRHTEMIQTYVEHI 179
Cdd:pfam03938   86 QKKQQELLQPIQDKINKA 103
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
72-186 1.24e-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: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   72 ENQEHEVElELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQeKKELQIQVEHYEfQTRQLE----LKAKNYADQI 147
Cdd:pfam13868   30 EKKRIKAE-EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIEERE-QKRQEEyeekLQEREQMDEI 106
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462548062  148 SRLEERESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  107 VERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEK 147
GreA_GreB_N pfam03449
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
469-496 1.29e-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: 1.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462548062  469 GELEAAKQAKVKLENRIKELEEELKRVK 496
Cdd:pfam03449   43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
450-570 1.29e-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: 39.90  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  450 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 526
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462548062  527 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 570
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
63-168 1.50e-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: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRR----QAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL 138
Cdd:pfam06785   85 FKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQiqlqQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRS 164
                           90       100       110
                   ....*....|....*....|....*....|
gi 2462548062  139 KAKNYADQISRLEERESEMKKEYNALHQRH 168
Cdd:pfam06785  165 VLEKRQDQIENLESKVRDLNYEIKTLLQLA 194
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
71-212 1.53e-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: 43.24  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   71 SENQEHEVELELLREDNEQLLTQYERekalRRQAEEkfiEFEDALEQEKKELQIQVEHYEFQ------TRQ--------L 136
Cdd:pfam01576   57 AEAEEMRARLAARKQELEEILHELES----RLEEEE---ERSQQLQNEKKKMQQHIQDLEEQldeeeaARQklqlekvtT 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548062  137 ELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQ--TESSLPGRSPRQSwrKSRKE 212
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeaMISDLEERLKKEE--KGRQE 205
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
897-979 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 2462548062  897 PSQSTEEATEATEVPDPGPSEPETATLRPGPltehVFTDPAPTPSSGPQP--GSENGPEPDSSSTRPEPEPSGDPTGAGS 974
Cdd:PRK07764   396 AAAPSAAAAAPAAAPAPAAAAPAAAAAPAPA----AAPQPAPAPAPAPAPpsPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471

                   ....*
gi 2462548062  975 SAAPT 979
Cdd:PRK07764   472 AAPEP 476
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
76-171 1.70e-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: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   76 HEVELELLREDNEQLLTQYEREKALRRQAEEKFI---------EFEDALEQEKKELQIQVEhyefqtrqlelkaknyadQ 146
Cdd:pfam12474   23 YEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIraeqkkrlkMFRESLKQEKKELKQEVE------------------K 84
                           90       100
                   ....*....|....*....|....*.
gi 2462548062  147 ISRLEERESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474   85 LPKFQRKEAKrQRKEELELEQKHEEL 110
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
63-187 2.01e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.52  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKALRRQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778   258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462548062  129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778   338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
435-581 2.02e-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: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  435 ENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVS 514
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548062  515 SYlctesdkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASREHPSVQEKKKSTI 581
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 2462548062   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALE-----QEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELE 152
                           90       100
                   ....*....|....*....|....*....
gi 2462548062  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 2462548062   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEkfiefedaLEQEKKELQIQVEHYEFQTRQLELKA-K 141
Cdd:COG4717    124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE--------LEAELAELQEELEELLEQLSLATEEElQ 195
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462548062  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. ...
451-498 2.08e-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: 2.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462548062  451 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSE 498
Cdd:pfam17675   44 EELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEE 91
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
53-179 2.14e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 40.54  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   53 KELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQ--YEREKALR--RQAEEKFIefEDALEQEKKELQIQVEH 128
Cdd:PRK14471    31 KPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEarAERDAILKeaREIKEKMI--ADAKEEAQVEGDKMIEQ 108
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548062  129 YEfQTRQLELKA-----KNYADQISrLEERESEMKKEYNALHQRHtEMIQTYVEHI 179
Cdd:PRK14471   109 AK-ASIESEKNAamaeiKNQVANLS-VEIAEKVLRKELSNKEKQH-KLVEKMLGDV 161
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
63-186 2.23e-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: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLS----------------ENQEHEVElELLREDNEQLLT------QYEREKA-LRRQAEEKfiefedalEQEK 119
Cdd:pfam01576  442 LESVSSLLNeaegkniklskdvsslESQLQDTQ-ELLQEETRQKLNlstrlrQLEDERNsLQEQLEEE--------EEAK 512
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548062  120 KELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ 186
Cdd:pfam01576  513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY-DKLEKTKnrLQQ 580
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
436-578 2.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 512
Cdd:COG4372     93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548062  513 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 578
Cdd:COG4372    169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
50-163 2.42e-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: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   50 EVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhy 129
Cdd:COG4942    139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-- 216
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462548062  130 efqtrQLELKAKNYADQISRLEERESEMKKEYNA 163
Cdd:COG4942    217 -----ELQQEAEELEALIARLEAEAAAAAERTPA 245
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
89-213 2.43e-03

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: 42.42  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   89 QLLTQYEREKAL-RRQAEEKFIEFE-DALEQEKKELQIQVEHY----EFQT-RQLEL--KAKNYADQISRLEERESEMKK 159
Cdd:pfam17380  273 QLLHIVQHQKAVsERQQQEKFEKMEqERLRQEKEEKAREVERRrkleEAEKaRQAEMdrQAAIYAEQERMAMERERELER 352
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462548062  160 EYNALHQRHTEMIQTYVEHIERSKMQQVgGNSQTESSLPGRSPRQSWRKSRKER 213
Cdd:pfam17380  353 IRQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVK 405
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
103-186 2.60e-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: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  103 QAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALHQRHTEM--IQTYVEH 178
Cdd:pfam10368   15 ELEKPFEEQQEPLvELEKKEQELYEEIIELGMDEFD-EIKKLSDEaLENVEEREELLEKEKESIEEAKEEFkkIKEIIEE 93

                   ....*...
gi 2462548062  179 IERSKMQQ 186
Cdd:pfam10368   94 IEDEELKK 101
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
74-183 2.63e-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: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   74 QEHEVELELLREDNEQLL----TQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868   87 QKRQEEYEEKLQEREQMDeiveRIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462548062  150 LEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-186 2.72e-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: 42.35  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYERE-KALRRQAeekfiefeDALEQEKKELQI-------QVEHYEFQ 132
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREAL--------DELRAELTLLNEeaanlreRLESLERR 832
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462548062  133 TRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEH-IERSKMQQ 186
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEE 887
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 2462548062   74 QEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELqiqvehyefqtRQLELKAKNYADQISRLEER 153
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-----------KRLELEIEEVEARIKKYEEQ 81
                           90
                   ....*....|...
gi 2462548062  154 ESEMK--KEYNAL 164
Cdd:COG1579     82 LGNVRnnKEYEAL 94
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
455-579 3.25e-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: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  455 AKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRV--KSEAIIARREP--------KEEAEDVSSYLCTESDKI 524
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrKIGEIEKEIEQleqeeeklKERLEELEEDLSSLEQEI 753
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462548062  525 PMAQRrrftrvEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 579
Cdd:TIGR02169  754 ENVKS------ELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
64-165 3.25e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQY--------EREKALRRQAEEkfiEFEDALEQEKKE------- 121
Cdd:PRK00409   516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELeekkeklqEEEDKLLEEAEK---EAQQAIKEAKKEadeiike 592
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462548062  122 --LQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409   593 lrQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
72-171 3.28e-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: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   72 ENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADqISRLE 151
Cdd:COG1196    688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELE 766
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462548062  152 ERESEMKK--------------EYNALHQRHTEM 171
Cdd:COG1196    767 RELERLEReiealgpvnllaieEYEELEERYDFL 800
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
73-186 3.43e-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: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   73 NQEHEVELELLREDNEQLltqyEREKALRRqaeekfiefEDALEQEKKELQIQVEHyefqtrqlELKAKNYADQISRLEE 152
Cdd:pfam15818  273 NTEMEAELKALKENNQTL----ERDNELQR---------EKVKENEEKFLNLQNEH--------EKALGTWKKHVEELNG 331
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462548062  153 RESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:pfam15818  332 EINEIKNELSSLKETHIKLQEHYNKLCNQKKFEE 365
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
464-512 3.76e-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: 3.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  464 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 512
Cdd:COG0711     33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
389-580 3.82e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  389 DSLYHELSTAGSEVIGDVDEGADLLGEFS-VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSG---EQ 464
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEA 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  465 EVLRGELEA----AKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSylcTESDKIPMAQRRRFTRVEMARV 540
Cdd:TIGR02168  781 EAEIEELEAqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESL 857
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462548062  541 LMERNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 580
Cdd:TIGR02168  858 AAEIEELEELIEELESELeALLNERASLEEALALLRSELEE 898
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
451-569 3.86e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  451 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSylctesdkipmaqrr 530
Cdd:COG4372     48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE--------------- 112
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462548062  531 rfTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 569
Cdd:COG4372    113 --LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
59-174 3.88e-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: 40.68  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   59 VVNVLENLDSVLSENQEHEVELELLRE----DNEQL--------LTQYERE----KALRRQAEEKFIEFEDALEQEKKEL 122
Cdd:COG1579     47 LEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLgnvrnnkeYEALQKEieslKRRISDLEDEILELMERIEELEEEL 126
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462548062  123 QiQVEhyefqtRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:COG1579    127 A-ELE------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
72-170 4.20e-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: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   72 ENQEHEVELELLRED----NEQLLTQYEREKAL---RRQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKAK 141
Cdd:pfam20492    7 EKQELEERLKQYEEEtkkaQEELEESEETAEELeeeRRQAEEEAERLEqkrQEAEEEKERLEESAEMEAEEKEQLEAELA 86
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462548062  142 NYADQISRLEE----RESEMKK-EYNALHQRHTE 170
Cdd:pfam20492   87 EAQEEIARLEEeverKEEEARRlQEELEEAREEE 120
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
906-977 4.33e-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: 4.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548062  906 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 977
Cdd:NF041121    17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
451-511 4.45e-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: 4.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548062  451 NDLIAKVDQLSGEQEVLRGELEaakqakvKLENRIKELEEELKRVKSEaiiARREPKEEAE 511
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 ...
464-512 4.74e-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: 4.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548062  464 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 512
Cdd:cd06503     32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
83-210 5.47e-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: 40.90  E-value: 5.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   83 LREDNEQLLTQYEREKALRRQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYN 162
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462548062  163 ALHQRHTEMIQTyvehierskMQQVGGNSQTESSLPGRSPRQSWRKSR 210
Cdd:COG4942    101 AQKEELAELLRA---------LYRLGRQPPLALLLSPEDFLDAVRRLQ 139
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 2462548062   74 QEHEVELELLREdnEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEER 153
Cdd:PRK12704    45 EEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
                           90       100
                   ....*....|....*....|
gi 2462548062  154 ESEMKKEYNALHQRHTEMIQ 173
Cdd:PRK12704   123 QQELEKKEEELEELIEEQLQ 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
63-181 5.59e-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: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462548062  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
Filament pfam00038
Intermediate filament protein;
419-569 5.72e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 40.29  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  419 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRV 495
Cdd:pfam00038   60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  496 KSEAIiarREPKEEAEDVSSYLctESDKIPmaqrrrftRVEMARVLME-RNQYKE---------------RLMELQEAV- 558
Cdd:pfam00038  140 HEEEV---RELQAQVSDTQVNV--EMDAAR--------KLDLTSALAEiRAQYEEiaaknreeaeewyqsKLEELQQAAa 206
                          170
                   ....*....|.
gi 2462548062  559 RWTEMIRASRE 569
Cdd:pfam00038  207 RNGDALRSAKE 217
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
79-159 5.87e-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: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   79 ELELLREDNEQLLTQYEREKAL------------RRQAEEK----FIEFEDALEQEKKelqiQVEHY--EFQTRQLELKA 140
Cdd:pfam05300   60 EEELRKKIKEELYKRLEQEQAKvqeelarlaereREAAQESltraILRERASTEDERL----KAQQLakQLEEKEAELKK 135
                           90       100
                   ....*....|....*....|.
gi 2462548062  141 KN--YADQISRLEERESEMKK 159
Cdd:pfam05300  136 QDafYKEQLARLEEKNAEFYK 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
63-181 6.85e-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: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   63 LENLDSVLSENQEhevELELLREDNEQLLTQYEREKALRRQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196    276 LEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEE 348
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462548062  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196    349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-181 7.21e-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: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFED---ALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196    288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEELEEAEEELEEAEAELAEAEEAL 367
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462548062  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 ...
437-558 7.45e-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: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  437 SQLLETKNALNVVKNDLIAKVDQLSgEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAiiarREPKEEAEDVSSY 516
Cdd:pfam04871    8 SEASSLKNENTELKAELQELSKQYN-SLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKE----KEKQSELDDLLLL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462548062  517 LCTESDKipmaqrrrftrvemarvlmeRNQYKERLMELQEAV 558
Cdd:pfam04871   83 LGDLEEK--------------------VEKYKARLKELGEEV 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
33-183 7.50e-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: 7.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   33 AGSIYREFERLIHCYDEEVVkELMPLVVNVLENLDSVLSENQEH-------EVELELLREDNEQLLTQYEREKALRRQAE 105
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALaneisrlEQQKQILRERLANLERQLEELEAQLEELE 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  106 EKFIEFED---ALEQEKKELQIQVE-------HYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRhtemIQTY 175
Cdd:TIGR02168  330 SKLDELAEelaELEEKLEELKEELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERL 405

                   ....*...
gi 2462548062  176 VEHIERSK 183
Cdd:TIGR02168  406 EARLERLE 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
432-557 7.91e-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: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  432 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARrepkeeae 511
Cdd:COG1196    230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LAR-------- 299
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462548062  512 dvssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 557
Cdd:COG1196    300 -------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-186 7.97e-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: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   65 NLDSVLSENQEHEVELELLREDN---EQLLTQYEREKALRRQAEEKFIEFEDALEQEKKEL-QIQVEHYEFQTRQLELKA 140
Cdd:COG4913    662 DVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAED 741
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462548062  141 KNYADQISRLEER---------ESEMKKEYNALHQRHTEMIQTYVEHIERsKMQQ 186
Cdd:COG4913    742 LARLELRALLEERfaaalgdavERELRENLEERIDALRARLNRAEEELER-AMRA 795
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
72-166 8.32e-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: 8.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   72 ENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKEL--------QIQVEHYEFQTRQLEL--KAK 141
Cdd:COG1196    317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaeaelaEAEEELEELAEELLEAlrAAA 396
                           90       100
                   ....*....|....*....|....*
gi 2462548062  142 NYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG1196    397 ELAAQLEELEEAEEALLERLERLEE 421
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
73-186 8.59e-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: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   73 NQEH----EVELELLREDNEQLLtQYEREKALR---------RQAEEKFIEFEDALEQEKKELQIQVEHYefqtrqlELK 139
Cdd:pfam13868  136 NEEQaewkELEKEEEREEDERIL-EYLKEKAEReeereaereEIEEEKEREIARLRAQQEKAQDEKAERD-------ELR 207
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462548062  140 AKNYADQISRlEERESEMKKEYNALHQRHtEMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  208 AKLYQEEQER-KERQKEREEAEKKARQRQ-ELQQAREEQIELKERRL 252
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
86-188 8.97e-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: 8.97e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062    86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82
                            90       100
                    ....*....|....*....|....*..
gi 2462548062   164 --LHQRHTEMIQTYVEHIERSkMQQVG 188
Cdd:smart00935   83 qdLQKRQQEELQKILDKINKA-IKEVA 108
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
443-509 9.78e-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: 9.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548062  443 KNALNVVKNDLIAKVDQLsgeqEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREpKEE 509
Cdd:pfam11221   59 EATQRELARDLILKAQQI----EYLIDSLPGIGVSEEEQLQRIKELEEELREAEEERQEAVKE-KEE 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
39-164 9.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062   39 EFERLIHCYDE------EVVKELMPLVvNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKAlRRQAEEKFIEFE 112
Cdd:PRK03918   294 EYIKLSEFYEEyldelrEIEKRLSRLE-EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKK 371
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548062  113 DALEQEKKELQI--------QVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNAL 164
Cdd:PRK03918   372 EELERLKKRLTGltpeklekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH