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Conserved domains on  [gi|741973655|ref|XP_010817425|]
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C-Jun-amino-terminal kinase-interacting protein 3 isoform X19 [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 29-184 2.76e-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: 240.21  E-value: 2.76e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741973655   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.
 919-1138 6.94e-47

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: 175.98  E-value: 6.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   919 QPEPEPSGDPAG-STSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGE 995
Cdd:pfam19056   84 EPEEEEAVRAERtAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAE 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   996 DGQWDLSNYHLMDLGHphHSIRCMAVVHDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLD 1075
Cdd:pfam19056  164 DGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSG 241

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741973655  1076 STLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1138
Cdd:pfam19056  242 SSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 384-452 1.20e-26

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: 103.93  E-value: 1.20e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741973655   384 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELR 452
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-519 2.67e-05

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEkfiefedaLEQEKKELQIQVEHYEFQTRQLELKA-K 141
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE--------LEAELAELQEELEELLEQLSLATEEElQ 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  142 NYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQQvggnsqtegslpgRRKERPTSLSVFPLAdgscpqd 221
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAA-------------ALEERLKEARLLLLI------- 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  222 emsesgqssAAATPSTTGTKSNTPTSSVPSAAVTPLSEGLQPLGDYGGSKNGKRAREKRNsrnmEVQVTQEMRNVsigmg 301
Cdd:COG4717   255 ---------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE----ELQALPALEEL----- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  302 SSDEWSDVQDIIDSTPELDMGREPRLDRTGSSpTQGIVNKAfgintDSLYHELSTAGSEvigdvDEGADLLGEFSVRDDf 381
Cdd:COG4717   317 EEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREA-----EELEEELQLEELE-----QEIAALLAEAGVEDE- 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  382 fgmgKEVGNLLLENSQLLETKNALNVVKNDLI-------------------AKVDQLSGEQEALKGDLEAARQAKLRLEN 442
Cdd:COG4717   385 ----EELRAALEQAEEYQELKEELEELEEQLEellgeleellealdeeeleEELEELEEELEELEEELEELREELAELEA 460

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  443 RIKDLEEElrRVKSEAITAHREPKEEVEDVSsclcteldkipmaqrRRFTRVEMARVLME--RNQYKERLME--LQEAVR 518
Cdd:COG4717   461 ELEQLEED--GELAELLQELEELKAELRELA---------------EEWAALKLALELLEeaREEYREERLPpvLERASE 523


                  .
gi 741973655  519 W 519
Cdd:COG4717   524 Y 524
PRK11633 super family cl25866
cell division protein DedD; Provisional
 854-937 2.94e-05

cell division protein DedD; Provisional


The actual alignment was detected with superfamily member PRK11633:

Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 46.92  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  854 VNPA-PST--EEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPP----STQPDSENGPEADVSgvqPEPEPSG 926
Cdd:PRK11633   59 ATQAlPTQppEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPkpveKPKPKPKPQQKVEAP---PAPKPEP 135

                          90
                  ....*....|.
gi 741973655  927 DPAGSTSAAPT 937
Cdd:PRK11633  136 KPVVEEKAAPT 146
 
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 2.76e-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: 240.21  E-value: 2.76e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741973655   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.
 919-1138 6.94e-47

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.98  E-value: 6.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   919 QPEPEPSGDPAG-STSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGE 995
Cdd:pfam19056   84 EPEEEEAVRAERtAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAE 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   996 DGQWDLSNYHLMDLGHphHSIRCMAVVHDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLD 1075
Cdd:pfam19056  164 DGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSG 241

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741973655  1076 STLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1138
Cdd:pfam19056  242 SSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 384-452 1.20e-26

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: 103.93  E-value: 1.20e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741973655   384 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELR 452
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 3.03e-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: 63.77  E-value: 3.03e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741973655   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKSLRKQ 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 1.76e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.80  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KSLRKQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741973655   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1012-1134 1.12e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 49.99  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655 1012 PHHSIRCMAVVHD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1084
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 741973655 1085 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLI-AGNRLWVGTGNGVVI 1134
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-519 2.67e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEkfiefedaLEQEKKELQIQVEHYEFQTRQLELKA-K 141
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE--------LEAELAELQEELEELLEQLSLATEEElQ 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  142 NYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQQvggnsqtegslpgRRKERPTSLSVFPLAdgscpqd 221
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAA-------------ALEERLKEARLLLLI------- 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  222 emsesgqssAAATPSTTGTKSNTPTSSVPSAAVTPLSEGLQPLGDYGGSKNGKRAREKRNsrnmEVQVTQEMRNVsigmg 301
Cdd:COG4717   255 ---------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE----ELQALPALEEL----- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  302 SSDEWSDVQDIIDSTPELDMGREPRLDRTGSSpTQGIVNKAfgintDSLYHELSTAGSEvigdvDEGADLLGEFSVRDDf 381
Cdd:COG4717   317 EEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREA-----EELEEELQLEELE-----QEIAALLAEAGVEDE- 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  382 fgmgKEVGNLLLENSQLLETKNALNVVKNDLI-------------------AKVDQLSGEQEALKGDLEAARQAKLRLEN 442
Cdd:COG4717   385 ----EELRAALEQAEEYQELKEELEELEEQLEellgeleellealdeeeleEELEELEEELEELEEELEELREELAELEA 460

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  443 RIKDLEEElrRVKSEAITAHREPKEEVEDVSsclcteldkipmaqrRRFTRVEMARVLME--RNQYKERLME--LQEAVR 518
Cdd:COG4717   461 ELEQLEED--GELAELLQELEELKAELRELA---------------EEWAALKLALELLEeaREEYREERLPpvLERASE 523


                  .
gi 741973655  519 W 519
Cdd:COG4717   524 Y 524
PRK11633 PRK11633
cell division protein DedD; Provisional
 854-937 2.94e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 46.92  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  854 VNPA-PST--EEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPP----STQPDSENGPEADVSgvqPEPEPSG 926
Cdd:PRK11633   59 ATQAlPTQppEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPkpveKPKPKPKPQQKVEAP---PAPKPEP 135

                          90
                  ....*....|.
gi 741973655  927 DPAGSTSAAPT 937
Cdd:PRK11633  136 KPVVEEKAAPT 146
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-219 3.36e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   74 QEHEVELELLREDNEQLLTQYEREKSLRKQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  152 ERE---SEMKKEYNALHQRHT--EMIQTYVEHIERSKmQQVGGNSQTE--------------------------GSLPGR 200
Cdd:PRK03918  342 ELKkklKELEKRLEELEERHElyEEAKAKKEELERLK-KRLTGLTPEKlekeleelekakeeieeeiskitariGELKKE 420

                         170
                  ....*....|....*....
gi 741973655  201 RKERPTSLSVFPLADGSCP 219
Cdd:PRK03918  421 IKELKKAIEELKKAKGKCP 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 395-521 1.64e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   395 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELRRVKSE---------AITAH 462
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqiaSLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   463 REP-KEEVEDVSSCLcTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTE 521
Cdd:TIGR02168  402 IERlEARLERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 1.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   79 ELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          90       100
                  ....*....|....*....|....*..
gi 741973655  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEA 402
Filament pfam00038
Intermediate filament protein;
378-528 1.91e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.83  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   378 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEE---LRRV 454
Cdd:pfam00038   60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   455 KSEAItahREPKEEVED------VSSCLCTELDKIpMAQRRRFTRVEMARVLME-RNQYKERLMELQEAV-RWTEMIRAS 526
Cdd:pfam00038  140 HEEEV---RELQAQVSDtqvnveMDAARKLDLTSA-LAEIRAQYEEIAAKNREEaEEWYQSKLEELQQAAaRNGDALRSA 215


                   ..
gi 741973655   527 RE 528
Cdd:pfam00038  216 KE 217
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 856-938 5.89e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.52  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  856 PAPSTEEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPPSTQPDSENGPEADVSGVQPEPEPSGDPAGSTSAA 935
Cdd:NF040712  225 GAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304


                  ...
gi 741973655  936 PTM 938
Cdd:NF040712  305 PAA 307
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-181 6.77e-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: 38.33  E-value: 6.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655     86 DNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|
gi 741973655    164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935   83 qdLQKRQQEELQKILDKINK 102
 
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 2.76e-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: 240.21  E-value: 2.76e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741973655   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.
 919-1138 6.94e-47

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.98  E-value: 6.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   919 QPEPEPSGDPAG-STSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGE 995
Cdd:pfam19056   84 EPEEEEAVRAERtAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAE 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   996 DGQWDLSNYHLMDLGHphHSIRCMAVVHDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLD 1075
Cdd:pfam19056  164 DGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSG 241

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741973655  1076 STLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLIAGNRLWVGTGNGVVISIPL 1138
Cdd:pfam19056  242 SSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 384-452 1.20e-26

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: 103.93  E-value: 1.20e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741973655   384 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELR 452
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 3.03e-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: 63.77  E-value: 3.03e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741973655   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKSLRKQ 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 1.76e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.80  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KSLRKQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741973655   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 39-185 1.09e-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: 49.85  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    39 EFERLIHCYDEEVvKELMPLVVNVleNLDSVLSENQEHEVELELLREdneqlltQYEREKSLRKQAEEKFIEFEDALEQ- 117
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLALLENL--ELDEAEEALEEIEERIDQLYD-------LLEKEVDAKKYVEKNLPEIEDYLEHa 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741973655   118 --EKKELQIQVEH----YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQ 185
Cdd:pfam06160  304 eeQNKELKEELERvqqsYTLNENELE-RVRGLEKQLEELEKRYDEIVERLEEKEVAYSE-LQEELEEILEQLEE 375
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1012-1134 1.12e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 49.99  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655 1012 PHHSIRCMAVVHD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1084
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 741973655 1085 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLI-AGNRLWVGTGNGVVI 1134
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 64-160 2.62e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKSLRKQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 741973655   123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523  492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-519 2.67e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEkfiefedaLEQEKKELQIQVEHYEFQTRQLELKA-K 141
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE--------LEAELAELQEELEELLEQLSLATEEElQ 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  142 NYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQQvggnsqtegslpgRRKERPTSLSVFPLAdgscpqd 221
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAA-------------ALEERLKEARLLLLI------- 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  222 emsesgqssAAATPSTTGTKSNTPTSSVPSAAVTPLSEGLQPLGDYGGSKNGKRAREKRNsrnmEVQVTQEMRNVsigmg 301
Cdd:COG4717   255 ---------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE----ELQALPALEEL----- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  302 SSDEWSDVQDIIDSTPELDMGREPRLDRTGSSpTQGIVNKAfgintDSLYHELSTAGSEvigdvDEGADLLGEFSVRDDf 381
Cdd:COG4717   317 EEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREA-----EELEEELQLEELE-----QEIAALLAEAGVEDE- 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  382 fgmgKEVGNLLLENSQLLETKNALNVVKNDLI-------------------AKVDQLSGEQEALKGDLEAARQAKLRLEN 442
Cdd:COG4717   385 ----EELRAALEQAEEYQELKEELEELEEQLEellgeleellealdeeeleEELEELEEELEELEEELEELREELAELEA 460

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  443 RIKDLEEElrRVKSEAITAHREPKEEVEDVSsclcteldkipmaqrRRFTRVEMARVLME--RNQYKERLME--LQEAVR 518
Cdd:COG4717   461 ELEQLEED--GELAELLQELEELKAELRELA---------------EEWAALKLALELLEeaREEYREERLPpvLERASE 523


                  .
gi 741973655  519 W 519
Cdd:COG4717   524 Y 524
PRK11633 PRK11633
cell division protein DedD; Provisional
 854-937 2.94e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 46.92  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  854 VNPA-PST--EEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPP----STQPDSENGPEADVSgvqPEPEPSG 926
Cdd:PRK11633   59 ATQAlPTQppEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPkpveKPKPKPKPQQKVEAP---PAPKPEP 135

                          90
                  ....*....|.
gi 741973655  927 DPAGSTSAAPT 937
Cdd:PRK11633  136 KPVVEEKAAPT 146
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-219 3.36e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   74 QEHEVELELLREDNEQLLTQYEREKSLRKQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  152 ERE---SEMKKEYNALHQRHT--EMIQTYVEHIERSKmQQVGGNSQTE--------------------------GSLPGR 200
Cdd:PRK03918  342 ELKkklKELEKRLEELEERHElyEEAKAKKEELERLK-KRLTGLTPEKlekeleelekakeeieeeiskitariGELKKE 420

                         170
                  ....*....|....*....
gi 741973655  201 RKERPTSLSVFPLADGSCP 219
Cdd:PRK03918  421 IKELKKAIEELKKAKGKCP 439
PRK12704 PRK12704
phosphodiesterase; Provisional
 72-223 7.36e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   72 ENQEHEVELELlREDNEQLLTQYEREKSLR----KQAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704   52 EAIKKEALLEA-KEEIHKLRNEFEKELRERrnelQKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  141 KNY----ADQISRLEE---------RE---SEMKKEynALHQRhTEMIQTYVEHIE-----RSK------MQQVGGNSQT 193
Cdd:PRK12704  131 EELeeliEEQLQELERisgltaeeaKEillEKVEEE--ARHEA-AVLIKEIEEEAKeeadkKAKeilaqaIQRCAADHVA 207

                         170       180       190
                  ....*....|....*....|....*....|
gi 741973655  194 EgslpgrrkerpTSLSVFPLadgscPQDEM 223
Cdd:PRK12704  208 E-----------TTVSVVNL-----PNDEM 221
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 7.91e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741973655  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 395-521 1.64e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   395 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELRRVKSE---------AITAH 462
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqiaSLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   463 REP-KEEVEDVSSCLcTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTE 521
Cdd:TIGR02168  402 IERlEARLERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 1.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   79 ELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          90       100
                  ....*....|....*....|....*..
gi 741973655  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEA 402
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 848-945 1.84e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  848 AVANGKVNPAPSTEEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPPSTQPDSENGPeADVSGVQPEPEPSGD 927
Cdd:PRK07764  409 APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA-APEPTAAPAPAPPAA 487

                          90
                  ....*....|....*...
gi 741973655  928 PAGSTSAAPTMWLGAQNG 945
Cdd:PRK07764  488 PAPAAAPAAPAAPAAPAG 505
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 66-185 1.88e-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: 44.94  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    66 LDSVLSENQEH--EVELELLREDNEQLLTQYEREKSLRKQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKa 140
Cdd:pfam09728  172 LQQATEEEEKKaqEKEVAKARELKAQVQTLSETEKELREQLNlyvEKFEEFQDTLNKSNEV---------FTTFKKEME- 241

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 741973655   141 kNYADQISRLEERESEMKKEYNALHQRHTEMI---QTYVEHIERSKMQ 185
Cdd:pfam09728  242 -KMSKKIKKLEKENLTWKRKWEKSNKALLEMAeerQKLKEELEKLQKK 288
PHA03247 PHA03247
large tegument protein UL36; Provisional
 827-924 2.20e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  827 RSNCSSRGDTPVLDKGQGEVSAVANGKVNPAPSTEEAteATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPtPPPSTQPD 906
Cdd:PHA03247  249 RGDIAAPAPPPVVGEGADRAPETARGATGPPPPPEAA--APNGAAAPPDGVWGAALAGAPLALPAPPDPPP-PAPAGDAE 325

                          90
                  ....*....|....*...
gi 741973655  907 SENGPEADVSGVQPEPEP 924
Cdd:PHA03247  326 EEDDEDGAMEVVSPLPRP 343
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-186 2.34e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4372    25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 741973655  138 LKAKNYADQISRLEEREsemkKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   105 SLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAERE 149
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-182 2.39e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   48 DEEVVKELMPLVVNVLENLDSVLSE--NQEHEVELELLREDNEQLLTQY--EREKSLRKQAEEKfiEFEDALEQEKKELQ 123
Cdd:COG4717   331 PPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQA--EEYQELKEELEELE 408

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741973655  124 IQVE-HYEFQTRQLE-LKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERS 182
Cdd:COG4717   409 EQLEeLLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAE-LEAELEQLEED 468
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-186 2.78e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   62 VLENLDSVLSENQEHEVELELLRED----NEQLLTQYEREKSLRKQAEEKFIEFEDA------LEQEKKELQIQVEHYEF 131
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEEleqaRSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741973655  132 QTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ 183
PRK12495 PRK12495
hypothetical protein; Provisional
 832-937 3.47e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 43.70  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  832 SRGDTPVLDKGQG-EVSAVANGKVNPAPSTEEATEATEVPDAGPSEAEAAAVRPgpltehvfTDPAPTPPPSTQPdseng 910
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTSA--------TDEAATDPPATAA----- 135

                          90       100
                  ....*....|....*....|....*..
gi 741973655  911 peadvSGVQPEPEPSGDPAGSTSAAPT 937
Cdd:PRK12495  136 -----ARDGPTPDPTAQPATPDERRSP 157
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-160 3.56e-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: 44.52  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    70 LSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE----QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312

                           90
                   ....*....|..
gi 741973655   150 -LEERESEMKKE 160
Cdd:pfam13868  313 eLEEGERLREEE 324
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-167 3.72e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 741973655  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 60-170 3.96e-04

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 41.86  E-value: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    60 VNVLENLDSVLSENQEHEVELELLREDNE---QLLTQ----YEREksLRKQAEEkfIEfedALEQEKKELQiqveHYEFQ 132
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaEIAREaqqnYERE--LVLHAED--IK---ALQALREELN----ELKAE 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 741973655   133 TRQLELKAKNYADQISRLE----ERESEMKKEYNALHQRHTE 170
Cdd:pfam07926   73 IAELKAEAESAKAELEESEesweEQKKELEKELSELEKRIED 114
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
410-528 6.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  410 NDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELRRVKSEAITAhrepKEEVEDVSsclcteldkipmaQRR 489
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA----QEELESLQ-------------EEA 110

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 741973655  490 RFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 528
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
Filament pfam00038
Intermediate filament protein;
66-185 6.27e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 6.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038   63 LDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKN 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 741973655   143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038  140 HEEEVRELQAQVSdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 39-160 6.68e-04

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


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.99  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   39 EFERLIHCYDEEVVKELMPLVVNVLENLdsvLSENQEhevelelLREDNEQL---LTQY-EREKSLRK---QAEEkfiEF 111
Cdd:COG3599    12 EFKKGFRGYDEDEVDEFLDEVAEDYERL---IRENKE-------LKEKLEELeeeLEEYrELEETLQKtlvVAQE---TA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 741973655  112 EDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEresEMKKE 160
Cdd:COG3599    79 EEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIE---ELKRQ 124
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-179 8.03e-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: 41.02  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    86 DNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL----KAKNYADQISRLEERESEMKKEY 161
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereeKEQELQKKEQELQQLQQKAQQEL 85

                           90
                   ....*....|....*...
gi 741973655   162 NALHQRHTEMIQTYVEHI 179
Cdd:pfam03938   86 QKKQQELLQPIQDKINKA 103
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 777-942 8.25e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 8.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  777 CISSIPAASDGDYPPGEIFldsDVNPEDSGADGVLAGITLVGCATRCNVPRS-NCSSRGDTPVLDKGQGEVSAVANGKVn 855
Cdd:PHA03307   19 EFFPRPPATPGDAADDLLS---GSQGQLVSDSAELAAVTVVAGAAACDRFEPpTGPPPGPGTEAPANESRSTPTWSLST- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  856 PAPSTEEATEATEVPDAGPSEAEAAAVRPGpltehvftDPAPTPPPSTQPDSENGPEADVSGVQPEPEPSGDPAGSTSAA 935
Cdd:PHA03307   95 LAPASPAREGSPTPPGPSSPDPPPPTPPPA--------SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDA 166


                  ....*..
gi 741973655  936 PTMWLGA 942
Cdd:PHA03307  167 ASSRQAA 173
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-183 8.99e-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: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    72 ENQEHEVELELLREDNEQL----LTQYEREKSLRKQAEEKFIEFEDALEQEKKELQIQV--EHYEFQTRQLELKAKNyad 145
Cdd:pfam13868   70 ERKRYRQELEEQIEEREQKrqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE--- 146

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 741973655   146 qisRLEERESEMK-KEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  147 ---KEEEREEDERiLEYLKEKAEREEEREAEREEIEEEK 182
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 63-168 9.76e-04

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


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 41.73  E-value: 9.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREK-SLRKQAE---EKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL 138
Cdd:pfam06785   85 FKILEETLEELQSEEERLEEELSQKEEELRRLTEENqQLQIQLQqisQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRS 164

                           90       100       110
                   ....*....|....*....|....*....|
gi 741973655   139 KAKNYADQISRLEERESEMKKEYNALHQRH 168
Cdd:pfam06785  165 VLEKRQDQIENLESKVRDLNYEIKTLLQLA 194
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 63-187 1.21e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.29  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKSLRKQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778  258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741973655  129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778  338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-170 1.28e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLELKAK- 141
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQl 402

                          90       100       110
                  ....*....|....*....|....*....|
gi 741973655  142 -NYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196   403 eELEEAEEALLERLERLEEELEELEEALAE 432
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 89-204 1.35e-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: 43.19  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    89 QLLTQYEREKSL-RKQAEEKFIEFE-DALEQEKKELQIQVEHY----EFQT-RQLEL--KAKNYADQISRLEERESEM-- 157
Cdd:pfam17380  273 QLLHIVQHQKAVsERQQQEKFEKMEqERLRQEKEEKAREVERRrkleEAEKaRQAEMdrQAAIYAEQERMAMERERELer 352

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 741973655   158 ------KKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTEGSLPGRRKER 204
Cdd:pfam17380  353 irqeerKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK 405
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 819-937 1.42e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  819 CAtRCNVPRSNCSSRGDTPVLDK-GQGEVSAVANGKVNPAPSTEEATEATEVPDAGPSEAEAAAVRPGPltehVFTDPAP 897
Cdd:PRK07764  359 CA-RMLLPSASDDERGLLARLERlERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPA----AAPQPAP 433

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 741973655  898 TPPPSTQPdsENGPEADVSGVQPEPEPSGDPAGSTSAAPT 937
Cdd:PRK07764  434 APAPAPAP--PSPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 391-516 1.43e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  391 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELRRVKSEAITAhrepkeeve 470
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--------- 300

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 741973655  471 dvssclctELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 516
Cdd:COG1196   301 --------EQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 72-186 1.44e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    72 ENQEHEVElELLREDNEQLLT------QYEREK-SLRKQAEEKfiefedalEQEKKELQIQVEHYEFQTRQLELKAKNYA 144
Cdd:pfam01576  467 ESQLQDTQ-ELLQEETRQKLNlstrlrQLEDERnSLQEQLEEE--------EEAKRNVERQLSTLQAQLSDMKKKLEEDA 537

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 741973655   145 DQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ 186
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAY-DKLEKTKnrLQQ 580
PHA03247 PHA03247
large tegument protein UL36; Provisional
 856-942 1.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  856 PAPSTEEATEATEVPDAGPSEAEAAAVRPGPL---TEHVFTDPAPTPPPSTQPDSENGPEADVsgvQPEPEPSGdpagst 932
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPERPPQPQAPPPPQpqpQPPPPPQPQPPPPPPPRPQPPLAPTTDP---AGAGEPSG------ 2957

                          90
                  ....*....|
gi 741973655  933 sAAPTMWLGA 942
Cdd:PHA03247 2958 -AVPQPWLGA 2966
Filament pfam00038
Intermediate filament protein;
378-528 1.91e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.83  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   378 RDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEE---LRRV 454
Cdd:pfam00038   60 RRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafLKKN 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   455 KSEAItahREPKEEVED------VSSCLCTELDKIpMAQRRRFTRVEMARVLME-RNQYKERLMELQEAV-RWTEMIRAS 526
Cdd:pfam00038  140 HEEEV---RELQAQVSDtqvnveMDAARKLDLTSA-LAEIRAQYEEIAAKNREEaEEWYQSKLEELQQAAaRNGDALRSA 215


                   ..
gi 741973655   527 RE 528
Cdd:pfam00038  216 KE 217
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 399-512 2.01e-03

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: 39.99  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   399 LETKNALNVVkNDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELRRVKSEAITAH---REPKEEVEDVSSC 475
Cdd:pfam11559   31 ENIARIINVI-YELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQakeRQLEKKLKTLEQK 109

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 741973655   476 LCTELD-----KIPMAQRRRFTRVEMARVLMERNQYKERLME 512
Cdd:pfam11559  110 LKNEKEelqrlKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 48-184 2.19e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    48 DEEVVKelmplvvnVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEE-------KFIEFED------- 113
Cdd:pfam01576   11 EEELQK--------VKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEmrarlaaRKQELEEilheles 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   114 ----------ALEQEKKELQIQVEHYEFQ------TRQ--------LELKAKNYADQISRLEERESEMKKEYNALHQRHT 169
Cdd:pfam01576   83 rleeeeersqQLQNEKKKMQQHIQDLEEQldeeeaARQklqlekvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162

                          170
                   ....*....|....*
gi 741973655   170 EMIQTYVEHIERSKM 184
Cdd:pfam01576  163 EFTSNLAEEEEKAKS 177
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 839-936 2.59e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  839 LDKGQGEVSAVANGKVNPAPSTEEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPPSTQPDSENGPEADVSGV 918
Cdd:PRK07764  381 LERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAA 460

                          90
                  ....*....|....*...
gi 741973655  919 QPEPEPSGDPAGSTSAAP 936
Cdd:PRK07764  461 APSAQPAPAPAAAPEPTA 478
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 88-186 2.76e-03

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


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    88 EQLLTQYEREKSLrkqaEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALH 165
Cdd:pfam10368    4 EKIYDHLEEAVEL----EKPFEEQQEPLvELEKKEQELYEEIIELGMDEFD-EIKKLSDEaLENVEEREELLEKEKESIE 78

                           90       100
                   ....*....|....*....|...
gi 741973655   166 QRHTEM--IQTYVEHIERSKMQQ 186
Cdd:pfam10368   79 EAKEEFkkIKEIIEEIEDEELKK 101
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 72-170 2.79e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.13  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    72 ENQEHEVELELLRED----NEQLLTQYEREKSL---RKQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKAK 141
Cdd:pfam20492    7 EKQELEERLKQYEEEtkkaQEELEESEETAEELeeeRRQAEEEAERLEqkrQEAEEEKERLEESAEMEAEEKEQLEAELA 86

                           90       100       110
                   ....*....|....*....|....*....|....
gi 741973655   142 NYADQISRLEE----RESEMKK-EYNALHQRHTE 170
Cdd:pfam20492   87 EAQEEIARLEEeverKEEEARRlQEELEEAREEE 120
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 49-180 2.85e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    49 EEVVKELMPLVVNVLENLDSVLSENQEHEVEL-----ELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQ 123
Cdd:TIGR04523  509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdledELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ 588

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741973655   124 IQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIE 180
Cdd:TIGR04523  589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSsiikniKSKKNKLKQEVKQIK 651
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 80-270 2.99e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   80 LELLREDNEQLLTQYereKSLRKQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKK 159
Cdd:COG3883   124 LSKIADADADLLEEL---KADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  160 EYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTEGSLPGRRKERPTSLSVFPLADGSCPQDEMSESGQSSAAATPSTTG 239
Cdd:COG3883   197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276

                         170       180       190
                  ....*....|....*....|....*....|.
gi 741973655  240 TKSNTPTSSVPSAAVTPLSEGLQPLGDYGGS 270
Cdd:COG3883   277 AAASAAGGGAGGAGGGGGGGGAASGGSGGGS 307
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 64-165 3.01e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQY--------EREKSLRKQAEEkfiEFEDALEQEKKE------- 121
Cdd:PRK00409  516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELeekkeklqEEEDKLLEEAEK---EAQQAIKEAKKEadeiike 592

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 741973655  122 --LQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409  593 lrQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
845-938 3.04e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  845 EVSAVANGKVNPAPSTEEATEATEVPdAGPSEAEAAAVRPGPL-TEHVFTDPAPTPPPsTQPDSENGPEADVSGVQPEPE 923
Cdd:PRK07003  392 GASAVPAVTAVTGAAGAALAPKAAAA-AAATRAEAPPAAPAPPaTADRGDDAADGDAP-VPAKANARASADSRCDERDAQ 469

                          90
                  ....*....|....*
gi 741973655  924 PSGDPAGSTSAAPTM 938
Cdd:PRK07003  470 PPADSGSASAPASDA 484
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 846-936 3.38e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.50  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  846 VSAVANGKVNPAPSTEEATEA-TEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPPSTQPDSENGPEADVSgvQPEPEP 924
Cdd:PRK13108  349 VVQVADRDGESTPAVEETSEAdIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKA--APIPDP 426

                          90
                  ....*....|..
gi 741973655  925 sGDPAGSTSAAP 936
Cdd:PRK13108  427 -AKPDELAVAGP 437
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 63-187 3.87e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    63 LENLDSVLSENQEhevELELLREDNEQLLTQYEREKSLRKQAEEKFIEFED----------ALEQEK-----KELQIQVE 127
Cdd:TIGR04523  241 INEKTTEISNTQT---QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqlkseisDLNNQKeqdwnKELKSELK 317

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741973655   128 HYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIER---SKMQQV 187
Cdd:TIGR04523  318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekQRELEEKQNEIEKLKKenqSYKQEI 386
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
396-537 3.91e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  396 SQLLETKNALNVVKNDLIAKVDQLSGEQEAL---KGDLEAARQAKLRLE-----------------NRIKDLEEELRRVK 455
Cdd:COG1340    74 KELKEERDELNEKLNELREELDELRKELAELnkaGGSIDKLRKEIERLEwrqqtevlspeeekelvEKIKELEKELEKAK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  456 sEAITAHREPKEevedvsscLCTELDKIpMAQRRRFTRvEMARVLMERNQYKERLMELQEAVrwtEMIRASRE--HPSVQ 533
Cdd:COG1340   154 -KALEKNEKLKE--------LRAELKEL-RKEAEEIHK-KIKELAEEAQELHEEMIELYKEA---DELRKEADelHKEIV 219


                  ....
gi 741973655  534 EKKK 537
Cdd:COG1340   220 EAQE 223
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 410-517 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 741973655  410 NDLIAKVDQLSGEQEALKGDLEAARQAKLRLENRIKDLEEELRRVKsEAITAHREPKeEVEDVSSclctELDKIpmAQRR 489
Cdd:COG1579    34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGNVRNNK-EYEALQK----EIESL--KRRI 105

                          90       100
                  ....*....|....*....|....*...
gi 741973655  490 RFTRVEMARVLMERNQYKERLMELQEAV 517
Cdd:COG1579   106 SDLEDEILELMERIEELEEELAELEAEL 133
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 396-517 4.28e-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: 38.53  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   396 SQLLETKNALNVVKNDLIAKVDQLSGEQEALKGdLEAARQAKLRLENRIKDLEEELRRVKSEAitahREPKEEVEDVSSC 475
Cdd:pfam04871    8 SEASSLKNENTELKAELQELSKQYNSLEQKESQ-AKELEAEVKKLEEALKKLKAELSEEKQKE----KEKQSELDDLLLL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 741973655   476 LCTELDKipmaqrrrftrvemarvlmeRNQYKERLMELQEAV 517
Cdd:pfam04871   83 LGDLEEK--------------------VEKYKARLKELGEEV 104
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 50-163 4.60e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   50 EVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQIQVEhy 129
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-- 216

                          90       100       110
                  ....*....|....*....|....*....|....
gi 741973655  130 efqtrQLELKAKNYADQISRLEERESEMKKEYNA 163
Cdd:COG4942   217 -----ELQQEAEELEALIARLEAEAAAAAERTPA 245
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
 52-209 4.69e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). 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: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 40.56  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    52 VKELMPLVVNVLENLDsvLSENQEhevELELLREDNEQLLtQYEREKSLRKQAeekfiEFEDALEQEKKElqiqvehyEF 131
Cdd:TIGR00570   99 LEEVEDIVYNLTNNID--LENTKK---KIETYQKENKDVI-QKNKEKSTREQE-----ELEEALEFEKEE--------EE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   132 QTRQLElkaknyadqisRLEERESEMKKEYNA------LHQRHTEMIQTYVEHIERSKMQqvggnsqtEGSLPGRRKERP 205
Cdd:TIGR00570  160 QRRLLL-----------QKEEEEQQMNKRKNKqalldeLETSTLPAAELIAQHKKNSVKL--------EMQVEKPKPEKP 220


                   ....
gi 741973655   206 TSLS 209
Cdd:TIGR00570  221 NTFS 224
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 74-164 4.82e-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: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   74 QEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELqiqvehyefqtRQLELKAKNYADQISRLEER 153
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-----------KRLELEIEEVEARIKKYEEQ 81

                          90
                  ....*....|...
gi 741973655  154 ESEMK--KEYNAL 164
Cdd:COG1579    82 LGNVRnnKEYEAL 94
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 846-936 5.04e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.24  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  846 VSAVANGKVNPAPSTEEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPPSTQPDSEngPEADVSGVQPEP--- 922
Cdd:PRK14951  396 QAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE--TVAIPVRVAPEPava 473

                          90
                  ....*....|....
gi 741973655  923 EPSGDPAGSTSAAP 936
Cdd:PRK14951  474 SAAPAPAAAPAAAR 487
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 76-171 5.33e-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: 38.70  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    76 HEVELELLREDNEQLLTQYEREKSLRKQAEEKFI---------EFEDALEQEKKELQIQVEhyefqtrqlelkaknyadQ 146
Cdd:pfam12474   23 YEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIraeqkkrlkMFRESLKQEKKELKQEVE------------------K 84

                           90       100
                   ....*....|....*....|....*.
gi 741973655   147 ISRLEERESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474   85 LPKFQRKEAKrQRKEELELEQKHEEL 110
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-181 5.67e-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: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFE-DALEQEKKELQIQVEHYEFQTRQL 136
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERERRRARLEALLAAL 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 741973655  137 ELK----AKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   372 GLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 856-938 5.89e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.52  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655  856 PAPSTEEATEATEVPDAGPSEAEAAAVRPGPLTEHVFTDPAPTPPPSTQPDSENGPEADVSGVQPEPEPSGDPAGSTSAA 935
Cdd:NF040712  225 GAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304


                  ...
gi 741973655  936 PTM 938
Cdd:NF040712  305 PAA 307
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 59-174 6.20e-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: 39.91  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   59 VVNVLENLDSVLSENQEHEVELELLRE----DNEQL--------LTQYERE----KSLRKQAEEKFIEFEDALEQEKKEL 122
Cdd:COG1579    47 LEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLgnvrnnkeYEALQKEieslKRRISDLEDEILELMERIEELEEEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 741973655  123 QiQVEhyefqtRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:COG1579   127 A-ELE------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 61-186 6.43e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 6.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655    61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYERE-KSLRKQAeekfiefeDALEQEKKELQI-------QVEHYEFQ 132
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREAL--------DELRAELTLLNEeaanlreRLESLERR 832

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 741973655   133 TRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEH-IERSKMQQ 186
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEE 887
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-181 6.77e-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: 38.33  E-value: 6.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655     86 DNEQLLTQYEREKSLRKQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|
gi 741973655    164 --LHQRHTEMIQTYVEHIER 181
Cdd:smart00935   83 qdLQKRQQEELQKILDKINK 102
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 67-194 6.85e-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: 40.25  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKSLRKQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269   169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 741973655  145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVGGNSQTE 194
Cdd:cd16269   237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEGFKEQAE 281
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-186 7.63e-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: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741973655   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKSLRKQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 741973655  141 KNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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