NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564370956|ref|XP_006246019|]
View 

C-Jun-amino-terminal kinase-interacting protein 3 isoform X6 [Rattus norvegicus]

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 3.92e-73

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: 239.82  E-value: 3.92e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564370956   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.
 955-1171 1.12e-46

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: 175.59  E-value: 1.12e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   955 EPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQW 1032
Cdd:pfam19056   88 EEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  1033 DLSNYHLMDLGHphHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLR 1112
Cdd:pfam19056  168 DPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIR 245

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956  1113 LYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1171
Cdd:pfam19056  246 LFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 425-493 3.25e-28

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: 108.55  E-value: 3.25e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956   425 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 493
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
436-569 4.61e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEaVTARREPREEVED 512
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQ 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564370956  513 DKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 569
Cdd:COG4372   172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
PRK12495 super family cl32772
hypothetical protein; Provisional
 864-968 2.38e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK12495:

Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 41.01  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  864 SRGDTPVLDKGQG-DVAATANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTqsSST 935
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPD--PTA 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564370956  936 QPASENGSESDGSIVQPQVEPSGESSATTSSAA 968
Cdd:PRK12495  147 QPATPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
 
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 3.92e-73

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: 239.82  E-value: 3.92e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564370956   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.
 955-1171 1.12e-46

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.59  E-value: 1.12e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   955 EPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQW 1032
Cdd:pfam19056   88 EEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  1033 DLSNYHLMDLGHphHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLR 1112
Cdd:pfam19056  168 DPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIR 245

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956  1113 LYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1171
Cdd:pfam19056  246 LFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 425-493 3.25e-28

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: 108.55  E-value: 3.25e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956   425 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 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 4.51e-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: 63.38  E-value: 4.51e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564370956   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRKQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-182 3.47e-06

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: 51.56  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRKQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564370956   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1045-1167 1.10e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 49.99  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956 1045 PHHSIRCMAVVDD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1117
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564370956 1118 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLI-AGNRLWVGTGNGVVI 1167
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
436-569 4.61e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEaVTARREPREEVED 512
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQ 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564370956  513 DKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 569
Cdd:COG4372   172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
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 564370956   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564370956  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 8.43e-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: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          90       100
                  ....*....|....*....|....*..
gi 564370956  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEA 402
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 435-572 2.73e-04

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: 45.44  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   435 ENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKrVKSEAVTARREPREEVEDDK 514
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE-DKALEIKKQEWKLEQLAADL 464

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564370956   515 IPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASREHPSVQEKKKSTI 572
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE--ERVRGGRAVEEVLKASI 520
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-548 4.13e-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: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  432 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAvtarreprEEVE 511
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------ARLE 301

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 564370956  512 DDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 548
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
Filament pfam00038
Intermediate filament protein;
419-560 1.38e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.21  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   419 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEE---LKRV 495
Cdd:pfam00038   60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   496 KSEAVtarREPREEVEDDKIpMAQRRRFTRVEMARVLME-RNQYKE---------------RLMELQEAV-RWTEMIRAS 558
Cdd:pfam00038  140 HEEEV---RELQAQVSDTQV-NVEMDAARKLDLTSALAEiRAQYEEiaaknreeaeewyqsKLEELQQAAaRNGDALRSA 215


                   ..
gi 564370956   559 RE 560
Cdd:pfam00038  216 KE 217
PRK12495 PRK12495
hypothetical protein; Provisional
 864-968 2.38e-03

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 41.01  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  864 SRGDTPVLDKGQG-DVAATANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTqsSST 935
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPD--PTA 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564370956  936 QPASENGSESDGSIVQPQVEPSGESSATTSSAA 968
Cdd:PRK12495  147 QPATPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
428-572 3.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  428 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---KGELEAAK-------QAKVKLENRIKELEEELK 493
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  494 RVKSEaVTARREPREEVEDDKiPMAQRRRftrvemaRVLMERNQYKERLMELQ-EAVRWTEMIRASREHPSVQEKKKSTI 572
Cdd:PRK03918  270 ELKKE-IEELEEKVKELKELK-EKAEEYI-------KLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-181 4.20e-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: 39.10  E-value: 4.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956     86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|
gi 564370956    164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935   83 qdLQKRQQEELQKILDKINK 102
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 864-948 4.43e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.92  E-value: 4.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   864 SRGDTPVldKGQGDVAATANGKVNPSQSTEEATEATEVPD--PGPSESEATTVRPGPLTEH------VFTDPA-PTQSSS 934
Cdd:pfam13254   37 SRQNSFA--SNRGSVAGPSGSLSPGLSPTKLSREGSPESTsrPSSSHSEATIVRHSKDDERpstpdeGFVKPAlPRHSRS 114

                           90
                   ....*....|....
gi 564370956   935 TQPASENGSESDGS 948
Cdd:pfam13254  115 SSALSNTGSEEDSP 128
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 417-510 7.83e-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: 40.82  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   417 SVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVK 496
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90
                   ....*....|....*.
gi 564370956   497 SE--AVTARREPREEV 510
Cdd:TIGR02169  758 SElkELEARIEELEED 773
 
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 3.92e-73

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: 239.82  E-value: 3.92e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564370956   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.
 955-1171 1.12e-46

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.59  E-value: 1.12e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   955 EPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQW 1032
Cdd:pfam19056   88 EEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  1033 DLSNYHLMDLGHphHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLR 1112
Cdd:pfam19056  168 DPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIR 245

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956  1113 LYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1171
Cdd:pfam19056  246 LFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 425-493 3.25e-28

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: 108.55  E-value: 3.25e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956   425 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELK 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 4.51e-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: 63.38  E-value: 4.51e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564370956   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRKQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-182 3.47e-06

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: 51.56  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRKQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564370956   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1045-1167 1.10e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 49.99  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956 1045 PHHSIRCMAVVDD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1117
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564370956 1118 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLI-AGNRLWVGTGNGVVI 1167
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 39-185 1.22e-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: 49.47  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    39 EFERLIHCYDEEVvKELMPLVVNVleNLDSVLSENQEHEVELELLREdneqlltQYEREKALRKQAEEKFIEFEDALEQ- 117
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLALLENL--ELDEAEEALEEIEERIDQLYD-------LLEKEVDAKKYVEKNLPEIEDYLEHa 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564370956   118 --EKKELQIQVEH----YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQ 185
Cdd:pfam06160  304 eeQNKELKEELERvqqsYTLNENELE-RVRGLEKQLEELEKRYDEIVERLEEKEVAYSE-LQEELEEILEQLEE 375
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
436-569 4.61e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEaVTARREPREEVED 512
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQ 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564370956  513 DKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 569
Cdd:COG4372   172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-160 6.26e-05

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: 46.84  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    70 LSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE----QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312

                           90
                   ....*....|..
gi 564370956   150 -LEERESEMKKE 160
Cdd:pfam13868  313 eLEEGERLREEE 324
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 564370956   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564370956  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 8.43e-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: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          90       100
                  ....*....|....*....|....*..
gi 564370956  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEA 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-167 1.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 564370956  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-182 1.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   48 DEEVVKELMPLVVNVLENLDSVLSE--NQEHEVELELLREDNEQLLTQY--EREKALRKQAEEKfiEFEDALEQEKKELQ 123
Cdd:COG4717   331 PPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQA--EEYQELKEELEELE 408

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370956  124 IQVE-HYEFQTRQLE-LKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERS 182
Cdd:COG4717   409 EQLEeLLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAE-LEAELEQLEED 468
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 64-160 2.04e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKALRKQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 564370956   123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523  492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 435-572 2.73e-04

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: 45.44  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   435 ENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKrVKSEAVTARREPREEVEDDK 514
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE-DKALEIKKQEWKLEQLAADL 464

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564370956   515 IPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASREHPSVQEKKKSTI 572
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE--ERVRGGRAVEEVLKASI 520
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 432-544 3.03e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 42.69  E-value: 3.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   432 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEeelKRVKSEAVTARREpREEVE 511
Cdd:pfam11559   43 LLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLE---KKLKTLEQKLKNE-KEELQ 118

                           90       100       110
                   ....*....|....*....|....*....|...
gi 564370956   512 DDKIPMAQRRRFTRVEMARVLMERNQYKERLME 544
Cdd:pfam11559  119 RLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-183 3.11e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   74 QEHEVELELLREDNEQLLTQYEREKALRKQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 564370956  152 ERE---SEMKKEYNALHQRHT--EMIQTYVEHIERSK 183
Cdd:PRK03918  342 ELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 66-185 4.03e-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: 4.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    66 LDSVLSENQEH--EVELELLREDNEQLLTQYEREKALRKQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKa 140
Cdd:pfam09728  172 LQQATEEEEKKaqEKEVAKARELKAQVQTLSETEKELREQLNlyvEKFEEFQDTLNKSNEV---------FTTFKKEME- 241

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 564370956   141 kNYADQISRLEERESEMKKEYNALHQRHTEMI---QTYVEHIERSKMQ 185
Cdd:pfam09728  242 -KMSKKIKKLEKENLTWKRKWEKSNKALLEMAeerQKLKEELEKLQKK 288
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
451-560 4.09e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  451 NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREpREEVEddkipmaQRRRFTRVEMAR 530
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-LESLQ-------EEAEELQEELEE 119

                          90       100       110
                  ....*....|....*....|....*....|
gi 564370956  531 VLMERNQYKERLMELQEAVRWTEMIRASRE 560
Cdd:COG4372   120 LQKERQDLEQQRKQLEAQIAELQSEIAERE 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-548 4.13e-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: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  432 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAvtarreprEEVE 511
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------ARLE 301

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 564370956  512 DDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 548
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-170 4.20e-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: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLELKAK- 141
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQl 402

                          90       100       110
                  ....*....|....*....|....*....|
gi 564370956  142 -NYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196   403 eELEEAEEALLERLERLEEELEELEEALAE 432
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-186 4.53e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4372    25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564370956  138 LKAKNYADQISRLEEREsemkKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   105 SLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 436-553 6.16e-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: 44.28  E-value: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   436 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREP---REE 509
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNE 401

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564370956   510 VE--DDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 553
Cdd:TIGR02168  402 IErlEARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
438-553 6.31e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  438 QLLETKNALNVVKNDLIAKVDQLsgEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDDKIPM 517
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564370956  518 AQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTE 553
Cdd:COG4913   344 EREIERLERELEERERRRARLEALLAALGLPLPASA 379
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-179 6.62e-04

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: 41.41  E-value: 6.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL----KAKNYADQISRLEERESEMKKEY 161
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereeKEQELQKKEQELQQLQQKAQQEL 85

                           90
                   ....*....|....*...
gi 564370956   162 NALHQRHTEMIQTYVEHI 179
Cdd:pfam03938   86 QKKQQELLQPIQDKINKA 103
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 60-167 6.83e-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: 41.09  E-value: 6.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    60 VNVLENLDSVLSENQEHEVELELLREDNE---QLLTQ----YERE--------KALRK------QAEEKFIEFEDALEQE 118
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaEIAREaqqnYERElvlhaediKALQAlreelnELKAEIAELKAEAESA 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 564370956   119 KKELQIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQR 167
Cdd:pfam07926   84 KAELEESEESWEEQKKELE-------KELSELEKRIEDLNEQNKLLHDQ 125
Filament pfam00038
Intermediate filament protein;
66-185 7.04e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 7.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038   63 LDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKN 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564370956   143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038  140 HEEEVRELQAQVSdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-186 8.11e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 8.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   62 VLENLDSVLSENQEHEVELELLRED----NEQLLTQYEREKALRKQAEEKFIEFEDA------LEQEKKELQIQVEHYEF 131
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEEleqaRSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564370956  132 QTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 430-548 9.38e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  430 GNLLLENSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREp 506
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA- 366

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 564370956  507 REEVEDDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 548
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 63-187 9.48e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKALRKQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778  258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564370956  129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778  338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-183 9.74e-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: 42.98  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    72 ENQEHEVELELLREDNEQL----LTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQV--EHYEFQTRQLELKAKNyad 145
Cdd:pfam13868   70 ERKRYRQELEEQIEEREQKrqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE--- 146

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 564370956   146 qisRLEERESEMK-KEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  147 ---KEEEREEDERiLEYLKEKAEREEEREAEREEIEEEK 182
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 39-225 1.05e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 43.41  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   39 EFERLIHCYDEEVVK---ELMPLVVNVLENLDSVLS--ENQEHEVELELLREDNEQLLTQYEREK----ALRKQAEEKFI 109
Cdd:COG5185   326 ELEESKRETETGIQNltaEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELDSFKDTIESTKesldEIPQNQRGYAQ 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  110 EFEDALEQEKKELQIQVEHY----EFQTRQLELKAKNYADQISRLEERESEMKKEYNA-LHQRHTEMIQTYVEHIERSKM 184
Cdd:COG5185   406 EILATLEDTLKAADRQIEELqrqiEQATSSNEEVSKLLNELISELNKVMREADEESQSrLEEAYDEINRSVRSKKEDLNE 485

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564370956  185 ------QQVGGGGQTESSLPGRSPRQ--SWRKSRKERPTSLNVFPLADG 225
Cdd:COG5185   486 eltqieSRVSTLKATLEKLRAKLERQleGVRSKLDQVAESLKDFMRARG 534
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 438-549 1.10e-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: 42.22  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  438 QLLETK-NALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTAR------REPRE-- 508
Cdd:COG1579    13 QELDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEye 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564370956  509 ----EVEDDKipmaQRRRFTRVEMARVLMERNQYKERLMELQEAV 549
Cdd:COG1579    93 alqkEIESLK----RRISDLEDEILELMERIEELEEELAELEAEL 133
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-166 1.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALE-----QEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELE 152

                          90       100
                  ....*....|....*....|....*....
gi 564370956  138 LKAKNYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEE 181
GreA_GreB_N pfam03449
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
 469-496 1.22e-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: 1.22e-03
                           10        20
                   ....*....|....*....|....*...
gi 564370956   469 GELEAAKQAKVKLENRIKELEEELKRVK 496
Cdd:pfam03449   43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
PRK12704 PRK12704
phosphodiesterase; Provisional
 72-152 1.25e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   72 ENQEHEVELELlREDNEQLLTQYEREKALR----KQAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704   52 EAIKKEALLEA-KEEIHKLRNEFEKELRERrnelQKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130

                          90
                  ....*....|....*.
gi 564370956  141 KNY----ADQISRLEE 152
Cdd:PRK12704  131 EELeeliEEQLQELER 146
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
453-561 1.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  453 LIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDDKIPMAQRRRFTRVEmARVl 532
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE-REL- 767

                          90       100       110
                  ....*....|....*....|....*....|.
gi 564370956  533 meRNQYKERLMELQEAVR--WTEMIRASREH 561
Cdd:COG4913   768 --RENLEERIDALRARLNraEEELERAMRAF 796
Filament pfam00038
Intermediate filament protein;
419-560 1.38e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.21  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   419 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEE---LKRV 495
Cdd:pfam00038   60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   496 KSEAVtarREPREEVEDDKIpMAQRRRFTRVEMARVLME-RNQYKE---------------RLMELQEAV-RWTEMIRAS 558
Cdd:pfam00038  140 HEEEV---RELQAQVSDTQV-NVEMDAARKLDLTSALAEiRAQYEEiaaknreeaeewyqsKLEELQQAAaRNGDALRSA 215


                   ..
gi 564370956   559 RE 560
Cdd:pfam00038  216 KE 217
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 39-160 1.57e-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: 39.84  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   39 EFERLIHCYDEEVVKELMPLVVNVLENLdsvLSENQEhevelelLREDNEQL---LTQY-EREKALRK---QAEEkfiEF 111
Cdd:COG3599    12 EFKKGFRGYDEDEVDEFLDEVAEDYERL---IRENKE-------LKEKLEELeeeLEEYrELEETLQKtlvVAQE---TA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564370956  112 EDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEresEMKKE 160
Cdd:COG3599    79 EEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIE---ELKRQ 124
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-186 1.91e-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: 42.21  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    72 ENQEHEVElELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQeKKELQIQVEHYEfQTRQLE----LKAKNYADQI 147
Cdd:pfam13868   30 EKKRIKAE-EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIEERE-QKRQEEyeekLQEREQMDEI 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 564370956   148 SRLEERESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  107 VERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEK 147
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
455-550 1.95e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  455 AKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEV-EDDKIPMAQRR--RFTRvEMARV 531
Cdd:COG2433   406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrKDREISRLDREieRLER-ELEEE 484

                          90
                  ....*....|....*....
gi 564370956  532 LMERNQYKERLMELQEAVR 550
Cdd:COG2433   485 RERIEELKRKLERLKELWK 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-186 2.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564370956  141 KNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-163 2.23e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883   121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                          90       100
                  ....*....|....*....|.
gi 564370956  143 YADQISRLEERESEMKKEYNA 163
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAA 214
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 63-168 2.26e-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: 40.96  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRK----QAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL 138
Cdd:pfam06785   85 FKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQiqlqQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRS 164

                           90       100       110
                   ....*....|....*....|....*....|
gi 564370956   139 KAKNYADQISRLEERESEMKKEYNALHQRH 168
Cdd:pfam06785  165 VLEKRQDQIENLESKVRDLNYEIKTLLQLA 194
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 35-217 2.28e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    35 SIYREFERLIHCYDEevVKELMPLVVNVLENL-----------DSVLSENQEHEVELELlrEDNEQLLTQYEREKALRKQ 103
Cdd:TIGR00618  567 EIQQSFSILTQCDNR--SKEDIPNLQNITVRLqdlteklseaeDMLACEQHALLRKLQP--EQDLQDVRLHLQQCSQELA 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   104 AEEKfiefedALEQEKKEL-QIQVEHYEFQTRQLELKAKnyadQISRLEERESEMKKEYNA-----LHQRHTEM--IQTY 175
Cdd:TIGR00618  643 LKLT------ALHALQLTLtQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTywkemLAQCQTLLreLETH 712

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 564370956   176 VEHIERSKMQQVGGGGQTESSLPGR--SPRQSWRKSRKERPTSL 217
Cdd:TIGR00618  713 IEEYDREFNEIENASSSLGSDLAARedALNQSLKELMHQARTVL 756
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 50-163 2.37e-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: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   50 EVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhy 129
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-- 216

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564370956  130 efqtrQLELKAKNYADQISRLEERESEMKKEYNA 163
Cdd:COG4942   217 -----ELQQEAEELEALIARLEAEAAAAAERTPA 245
PRK12495 PRK12495
hypothetical protein; Provisional
 864-968 2.38e-03

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 41.01  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  864 SRGDTPVLDKGQG-DVAATANGKVNPSQSTEEATEATEVPDPGPSESEA-------TTVRPGPLTEHVFTDPAPTqsSST 935
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEAsstsatdEAATDPPATAAARDGPTPD--PTA 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564370956  936 QPASENGSESDGSIVQPQVEPSGESSATTSSAA 968
Cdd:PRK12495  147 QPATPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 455-570 2.63e-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: 42.36  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   455 AKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPR-------------EEVEDDKIPMAQRR 521
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqeeeklkerlEELEEDLSSLEQEI 753

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 564370956   522 RFTRVEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 570
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 389-571 2.75e-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: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   389 DSLYHELSTAGSEVIGDVDEGADLLGEFS-VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSG----- 462
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaea 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   463 --EQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEA--VTARREPREEVEDDKIPM----AQRRRFTRVEMARVLME 534
Cdd:TIGR02168  781 eaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanLRERLESLERRIAATERRledlEEQIEELSEDIESLAAE 860

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 564370956   535 RNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 571
Cdd:TIGR02168  861 IEELEELIEELESELeALLNERASLEEALALLRSELEE 898
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 74-164 2.76e-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: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   74 QEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELqiqvehyefqtRQLELKAKNYADQISRLEER 153
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-----------KRLELEIEEVEARIKKYEEQ 81

                          90
                  ....*....|...
gi 564370956  154 ESEMK--KEYNAL 164
Cdd:COG1579    82 LGNVRnnKEYEAL 94
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-181 2.84e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFE-DALEQEKKELQIQVEHYEFQTRQL 136
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERERRRARLEALLAAL 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564370956  137 ELK----AKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   372 GLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 451-498 2.86e-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: 39.12  E-value: 2.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564370956   451 NDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSE 498
Cdd:pfam17675   44 EELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEE 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-548 2.99e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  432 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREpREEVE 511
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELA 399

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 564370956  512 DDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 548
Cdd:COG1196   400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
428-572 3.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  428 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---KGELEAAK-------QAKVKLENRIKELEEELK 493
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  494 RVKSEaVTARREPREEVEDDKiPMAQRRRftrvemaRVLMERNQYKERLMELQ-EAVRWTEMIRASREHPSVQEKKKSTI 572
Cdd:PRK03918  270 ELKKE-IEELEEKVKELKELK-EKAEEYI-------KLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 72-186 3.06e-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: 42.08  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    72 ENQEHEVElELLREDNEQLLT------QYEREKA-LRKQAEEKfiefedalEQEKKELQIQVEHYEFQTRQLELKAKNYA 144
Cdd:pfam01576  467 ESQLQDTQ-ELLQEETRQKLNlstrlrQLEDERNsLQEQLEEE--------EEAKRNVERQLSTLQAQLSDMKKKLEEDA 537

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 564370956   145 DQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ 186
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAY-DKLEKTKnrLQQ 580
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 464-560 3.14e-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: 42.03  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   464 QEVLKGELEAAKQAKVKLENRIKELEEELK-RVKSEAVTARREPREEVEDDKIPMAQRRRFTRvEMARVLMERNQYK--E 540
Cdd:pfam17380  494 RKILEKELEERKQAMIEEERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRRIQE-QMRKATEERSRLEamE 572

                           90       100
                   ....*....|....*....|
gi 564370956   541 RLMELQEAVRWTEMIRASRE 560
Cdd:pfam17380  573 REREMMRQIVESEKARAEYE 592
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-183 3.48e-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: 41.06  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    70 LSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFI-EFEDALEQ--EKKELQIQvehyefQTRQLELKAKNYADQ 146
Cdd:pfam13868   90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLReEIDEFNEEqaEWKELEKE------EEREEDERILEYLKE 163

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 564370956   147 ISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 67-188 3.77e-03

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: 41.02  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKALRKQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269   169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564370956  145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVG 188
Cdd:cd16269   237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEG 275
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 64-165 3.89e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQYEREKALRKQAEEKFI-----EFEDALEQEKKE---------L 122
Cdd:PRK00409  516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLeeaekEAQQAIKEAKKEadeiikelrQ 595

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 564370956  123 QIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409  596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 59-174 3.96e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   59 VVNVLENLDSVLSENQEHEVELELLRE----DNEQL--------LTQYERE----KALRKQAEEKFIEFEDALEQEKKEL 122
Cdd:COG1579    47 LEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLgnvrnnkeYEALQKEieslKRRISDLEDEILELMERIEELEEEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564370956  123 QiQVEhyefqtRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:COG1579   127 A-ELE------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 71-184 4.01e-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: 41.70  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    71 SENQEHEVELELLREDNEQLLTQYERekalRKQAEEkfiEFEDALEQEKKELQIQVEHYEFQ------TRQ--------L 136
Cdd:pfam01576   57 AEAEEMRARLAARKQELEEILHELES----RLEEEE---ERSQQLQNEKKKMQQHIQDLEEQldeeeaARQklqlekvtT 129

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 564370956   137 ELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKM 184
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS 177
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 76-171 4.19e-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: 39.08  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    76 HEVELELLREDNEQLLTQYEREKALRKQAEEKFI---------EFEDALEQEKKELQIQVEhyefqtrqlelkaknyadQ 146
Cdd:pfam12474   23 YEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIraeqkkrlkMFRESLKQEKKELKQEVE------------------K 84

                           90       100
                   ....*....|....*....|....*.
gi 564370956   147 ISRLEERESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474   85 LPKFQRKEAKrQRKEELELEQKHEEL 110
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-181 4.20e-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: 39.10  E-value: 4.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956     86 DNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|
gi 564370956    164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935   83 qdLQKRQQEELQKILDKINK 102
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-186 4.26e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQlelKAKN 142
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLATEE---ELQD 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564370956  143 YADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQQ 186
Cdd:COG4717   197 LAEELEELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAA 239
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1045-1167 4.42e-03

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 41.51  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956 1045 PHHSIRCMAV-VDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDG-VWVSirLDSTLRLYHAHTHQhl 1122
Cdd:COG3292    79 PSNYIRALLEdSDGRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGnIWVG--TSNGLYRYDPKTGK-- 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564370956 1123 qdvdIEPYVSKmlgtgklGFSFVRITALLIAGN---------RLWVGT-GNGVVI 1167
Cdd:COG3292   155 ----FKRFTLD-------GLPSNTITSLAEDADgnlwvdsdgNLWIGTdGNGLYR 198
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 864-948 4.43e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.92  E-value: 4.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   864 SRGDTPVldKGQGDVAATANGKVNPSQSTEEATEATEVPD--PGPSESEATTVRPGPLTEH------VFTDPA-PTQSSS 934
Cdd:pfam13254   37 SRQNSFA--SNRGSVAGPSGSLSPGLSPTKLSREGSPESTsrPSSSHSEATIVRHSKDDERpstpdeGFVKPAlPRHSRS 114

                           90
                   ....*....|....
gi 564370956   935 TQPASENGSESDGS 948
Cdd:pfam13254  115 SSALSNTGSEEDSP 128
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 97-186 4.63e-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: 39.50  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    97 EKAlrKQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALHQRHTEM--I 172
Cdd:pfam10368   11 EEA--VELEKPFEEQQEPLvELEKKEQELYEEIIELGMDEFD-EIKKLSDEaLENVEEREELLEKEKESIEEAKEEFkkI 87

                           90
                   ....*....|....
gi 564370956   173 QTYVEHIERSKMQQ 186
Cdd:pfam10368   88 KEIIEEIEDEELKK 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 61-186 5.64e-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: 41.20  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYERE-KALRKQAeekfiefeDALEQEKKELQI-------QVEHYEFQ 132
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREAL--------DELRAELTLLNEeaanlreRLESLERR 832

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564370956   133 TRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEH-IERSKMQQ 186
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEE 887
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-166 5.84e-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: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   72 ENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKEL--------QIQVEHYEFQTRQLEL--KAK 141
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaeaelaEAEEELEELAEELLEAlrAAA 396

                          90       100
                  ....*....|....*....|....*
gi 564370956  142 NYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEE 421
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 450-561 6.13e-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: 37.98  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   450 KNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEE---LKRVKSEAVTARREPREEVEDDKIpmaqrrrfTRV 526
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEMEAE--------EKE 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 564370956   527 EMARVLMERNQYKERLMEL-----QEAVRW-TEMIRASREH 561
Cdd:pfam20492   80 QLEAELAEAQEEIARLEEEverkeEEARRLqEELEEAREEE 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
39-164 6.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   39 EFERLIHCYDE------EVVKELMPLVvNVLENLDSVLSENQEHEVELELLREDNEQLLTQYER--------EKALRKQA 104
Cdd:PRK03918  294 EYIKLSEFYEEyldelrEIEKRLSRLE-EEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKE 372

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  105 EEKFIEFEDAlEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNAL 164
Cdd:PRK03918  373 ELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
459-576 6.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  459 QLSGEQEVLKgELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDDKIPMAQRRRFTRVEMARVLMERNQY 538
Cdd:COG4717   140 ELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 564370956  539 KERLMELQEAVrwtEMIRASREHPSVQEKKKSTIWQFF 576
Cdd:COG4717   219 QEELEELEEEL---EQLENELEAAALEERLKEARLLLL 253
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 419-560 6.41e-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: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  419 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSE 498
Cdd:COG1196   287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564370956  499 AVTARREPREEVEDDkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRwtEMIRASRE 560
Cdd:COG1196   367 LLEAEAELAEAEEEL----EELAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEE 422
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-186 6.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   65 NLDSVLSENQEHEVELELLREDN---EQLLTQYEREKALRKQAEEKFIEFEDALEQEKKEL-QIQVEHYEFQTRQLELKA 140
Cdd:COG4913   662 DVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAED 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564370956  141 KNYADQISRLEER---------ESEMKKEYNALHQRHTEMIQTYVEHIERsKMQQ 186
Cdd:COG4913   742 LARLELRALLEERfaaalgdavERELRENLEERIDALRARLNRAEEELER-AMRA 795
PRK10856 PRK10856
cytoskeleton protein RodZ;
888-1005 6.54e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956  888 PSQSTEEATEATEVPDPGPSESEATTVRPGPLTehvftdpAPTQSSSTQPASENGSESDGSIVQPQVEPSGESSATTSSA 967
Cdd:PRK10856  170 TDPATTPAPAAPVDTTPTNSQTPAVATAPAPAV-------DPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQA 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 564370956  968 APTMWLGAQNG---------WLYVHSavANWKKCLHSIKLKDSVLSL 1005
Cdd:PRK10856  243 GVSTPAADPNAlvmnftadcWLEVTD--ATGKKLFSGMQRKGGNLNL 287
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 72-170 6.68e-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: 37.98  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    72 ENQEHEVELELLRED----NEQLLTQYEREKAL---RKQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKAK 141
Cdd:pfam20492    7 EKQELEERLKQYEEEtkkaQEELEESEETAEELeeeRRQAEEEAERLEqkrQEAEEEKERLEESAEMEAEEKEQLEAELA 86

                           90       100       110
                   ....*....|....*....|....*....|....
gi 564370956   142 NYADQISRLEE----RESEMKK-EYNALHQRHTE 170
Cdd:pfam20492   87 EAQEEIARLEEeverKEEEARRlQEELEEAREEE 120
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 437-549 6.92e-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: 38.15  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   437 SQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKvKLENRIKELEEELKRVKSEAvtarREPREEVEDDKIP 516
Cdd:pfam04871    8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVK-KLEEALKKLKAELSEEKQKE----KEKQSELDDLLLL 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 564370956   517 MAQrrrftrvEMARvlmeRNQYKERLMELQEAV 549
Cdd:pfam04871   83 LGD-------LEEK----VEKYKARLKELGEEV 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 417-510 7.83e-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: 40.82  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   417 SVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVK 496
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90
                   ....*....|....*.
gi 564370956   497 SE--AVTARREPREEV 510
Cdd:TIGR02169  758 SElkELEARIEELEED 773
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-181 7.85e-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: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564370956  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 79-159 8.86e-03

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


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 38.52  E-value: 8.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956    79 ELELLREDNEQLLTQYEREKALRKQAEEKFIEFE---------DALEQEK----KELQiQVEHY--EFQTRQLELKAKN- 142
Cdd:pfam05300   60 EEELRKKIKEELYKRLEQEQAKVQEELARLAEREreaaqesltRAILRERasteDERL-KAQQLakQLEEKEAELKKQDa 138

                           90
                   ....*....|....*...
gi 564370956   143 -YADQISRLEERESEMKK 159
Cdd:pfam05300  139 fYKEQLARLEEKNAEFYK 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-181 9.38e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   63 LENLDSVLSENQEhevELELLREDNEQLLTQYEREKALRKQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   276 LEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEE 348

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564370956  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-171 9.54e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370956   72 ENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADqISRLE 151
Cdd:COG1196   688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELE 766

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564370956  152 ERESEMKK--------------EYNALHQRHTEM 171
Cdd:COG1196   767 RELERLEReiealgpvnllaieEYEELEERYDFL 800
 
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