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Conserved domains on  [gi|767987055|ref|XP_011520732|]
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C-Jun-amino-terminal kinase-interacting protein 3 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 29-184 9.04e-74

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


:

Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 241.75  E-value: 9.04e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987055   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.
 950-1174 1.07e-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: 178.67  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   950 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1027
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  1028 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1107
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987055  1108 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1174
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 419-487 4.99e-29

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


:

Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 110.86  E-value: 4.99e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987055   419 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 487
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 845-959 1.06e-09

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


:

Pssm-ID: 368653  Cd Length: 134  Bit Score: 57.88  E-value: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   845 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 921
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767987055   922 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 959
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 399-575 1.43e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   399 GSEVIGDVDEGADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENR 478
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   479 IKELEEELKRVKSEAIIARREPKEEAEDVSSYlctesdkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmi 558
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWKLEQLAADLSKY----------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE-- 503

                          170
                   ....*....|....*..
gi 767987055   559 RASREHPSVQEKKKSTI 575
Cdd:TIGR02169  504 ERVRGGRAVEEVLKASI 520
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-310 5.18e-04

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883   121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRSPRQSWRKSRKERPTSLNVF 220
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  221 PLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNES 300
Cdd:COG3883   274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353

                         250
                  ....*....|
gi 767987055  301 LQPLGDYGVG 310
Cdd:COG3883   354 GGGGSSSGGG 363
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 29-184 9.04e-74

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 241.75  E-value: 9.04e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987055   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.
 950-1174 1.07e-47

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 178.67  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   950 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1027
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  1028 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1107
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987055  1108 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1174
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 419-487 4.99e-29

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 110.86  E-value: 4.99e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987055   419 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 487
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 1.99e-12

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 64.15  E-value: 1.99e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987055   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRRQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 845-959 1.06e-09

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


Pssm-ID: 368653  Cd Length: 134  Bit Score: 57.88  E-value: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   845 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 921
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767987055   922 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 959
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-182 6.97e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRRQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767987055   126 VEHYEFQTRQLE-------------------LKAKNY--ADQISRLEERESEMKKEYNALHQRhTEMIQTYVEHIERS 182
Cdd:TIGR04523  400 IQNQEKLNQQKDeqikklqqekellekeierLKETIIknNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRS 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-167 4.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 767987055  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1048-1170 5.90e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055 1048 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1120
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767987055 1121 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 1170
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 7.25e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767987055  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK11633 PRK11633
cell division protein DedD; Provisional
 891-978 8.62e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.38  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  891 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 965
Cdd:PRK11633   64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143

                          90
                  ....*....|...
gi 767987055  966 AGSSAAPTMWLGA 978
Cdd:PRK11633  144 APTGKAYVVQLGA 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 399-575 1.43e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   399 GSEVIGDVDEGADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENR 478
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   479 IKELEEELKRVKSEAIIARREPKEEAEDVSSYlctesdkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmi 558
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWKLEQLAADLSKY----------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE-- 503

                          170
                   ....*....|....*..
gi 767987055   559 RASREHPSVQEKKKSTI 575
Cdd:TIGR02169  504 ERVRGGRAVEEVLKASI 520
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-310 5.18e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883   121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRSPRQSWRKSRKERPTSLNVF 220
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  221 PLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNES 300
Cdd:COG3883   274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353

                         250
                  ....*....|
gi 767987055  301 LQPLGDYGVG 310
Cdd:COG3883   354 GGGGSSSGGG 363
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 445-525 1.04e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  445 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 514
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596

                          90
                  ....*....|.
gi 767987055  515 SDKIPMAQRRR 525
Cdd:PRK00409  597 QKGGYASVKAH 607
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 444-564 1.38e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.90  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   444 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 520
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767987055   521 AQRRRFTRVEMARVLMERNQYKERLMELQEavrwtEMIRASREH 564
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVERKEEEARRLQE-----ELEEAREEE 120
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
 390-494 2.51e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153284 [Multi-domain]  Cd Length: 242  Bit Score: 41.19  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  390 SLYHELS---TAGSEVIG-----DVDEGADLLGEFSGMGKEVGNLLLENSQLLETK-NA-LNVVKNDLIAKVDQLSGEQE 459
Cdd:cd07600    78 TLNHALSraaLASSLELKslepeDEDPLSKALGKYSDAEEKIAEARLEQDQLIQKEfNAkLRETLNTSFQKAHKARKKVE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767987055  460 VLRGELEAAKQAKVKLENRIKE---------LEEELKRVKSEAI 494
Cdd:cd07600   158 DKRLQLDTARAELKSAEPAEKQeaarvevetAEDEFVSATEEAV 201
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
430-572 2.51e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  430 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 506
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987055  507 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 572
Cdd:COG4372   169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 458-506 3.82e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.39  E-value: 3.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767987055  458 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 506
Cdd:COG0711    33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 900-971 4.35e-03

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 41.14  E-value: 4.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987055  900 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 971
Cdd:NF041121   17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-188 9.27e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 9.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055     86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|....*..
gi 767987055    164 --LHQRHTEMIQTYVEHIERSkMQQVG 188
Cdd:smart00935   83 qdLQKRQQEELQKILDKINKA-IKEVA 108
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 29-184 9.04e-74

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 241.75  E-value: 9.04e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    29 VSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKF 108
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987055   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.
 950-1174 1.07e-47

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 178.67  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   950 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 1027
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  1028 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 1107
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987055  1108 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 1174
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 419-487 4.99e-29

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 110.86  E-value: 4.99e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987055   419 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 487
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 1.99e-12

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 64.15  E-value: 1.99e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987055   32 LAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLltqyEREKALRRQ 103
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQ 88
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 845-959 1.06e-09

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


Pssm-ID: 368653  Cd Length: 134  Bit Score: 57.88  E-value: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   845 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 921
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767987055   922 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 959
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-182 6.97e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    61 NVLENLDSVLSENQEH-----------EVELELLREDNEQL---LTQYERE-KALRRQAEEKFIEFEDaLEQEKKELQIQ 125
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIisqlneqisqlKKELTNSESENSEKqreLEEKQNEiEKLKKENQSYKQEIKN-LESQINDLESK 399

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767987055   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 1.62e-05

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 49.08  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    39 EFERLIHCYDEEVvKELMPLVVNVleNLDSVLSENQEHEVELELLREdneqlltQYEREKALRRQAEEKFIEFEDALEQ- 117
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLALLENL--ELDEAEEALEEIEERIDQLYD-------LLEKEVDAKKYVEKNLPEIEDYLEHa 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987055   118 --EKKELQIQVEH----YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQ 185
Cdd:pfam06160  304 eeQNKELKEELERvqqsYTLNENELE-RVRGLEKQLEELEKRYDEIVERLEEKEVAYSE-LQEELEEILEQLEE 375
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-167 4.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQI---QVEHYEFQTRQLELKAKN 142
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 767987055  143 YADQISRLEERESEMKKEYNALHQR 167
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
1048-1170 5.90e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055 1048 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 1120
Cdd:COG3292   265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767987055 1121 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 1170
Cdd:COG3292   343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-164 7.25e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   33 AGSIYREFERLIHCYDEEVVKE--LMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIE 110
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767987055  111 FEdALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEREsEMKKEYNAL 164
Cdd:PRK03918  247 LE-SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKL 298
PRK11633 PRK11633
cell division protein DedD; Provisional
 891-978 8.62e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.38  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  891 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 965
Cdd:PRK11633   64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143

                          90
                  ....*....|...
gi 767987055  966 AGSSAAPTMWLGA 978
Cdd:PRK11633  144 APTGKAYVVQLGA 156
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-181 8.67e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 8.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   79 ELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQ----EKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERE 154
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          90       100
                  ....*....|....*....|....*..
gi 767987055  155 SEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEA 402
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-182 1.03e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   48 DEEVVKELMPLVVNVLENLDSVLSE--NQEHEVELELLREDNEQLLTQY--EREKALRRQAEEKfiEFEDALEQEKKELQ 123
Cdd:COG4717   331 PPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQA--EEYQELKEELEELE 408

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987055  124 IQVE-HYEFQTRQLE-LKAKNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERS 182
Cdd:COG4717   409 EQLEeLLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAE-LEAELEQLEED 468
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-160 1.06e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    70 LSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEfedaLEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE----QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312

                           90
                   ....*....|..
gi 767987055   150 -LEERESEMKKE 160
Cdd:pfam13868  313 eLEEGERLREEE 324
Filament pfam00038
Intermediate filament protein;
66-185 1.36e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.68  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    66 LDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE---DALEQEKKELQIQVEHYefqTRQLELKAKN 142
Cdd:pfam00038   63 LDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKN 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767987055   143 YADQISRLEERES------EMKkeyNALHQRHT----EMIQTYVEHIERSKMQ 185
Cdd:pfam00038  140 HEEEVRELQAQVSdtqvnvEMD---AARKLDLTsalaEIRAQYEEIAAKNREE 189
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 64-160 1.37e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    64 ENLDSVLSENQEHEVELELLREDNEQ--------------LLTQYEREKALRRQAEEKFIEFEDA-------LEQEKKEL 122
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKEL 491

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 767987055   123 QIQV-EHYEF--QTRQLELKAKNYADQISRLEERESEMKKE 160
Cdd:TIGR04523  492 KSKEkELKKLneEKKELEEKVKDLTKKISSLKEKIEKLESE 532
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 399-575 1.43e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   399 GSEVIGDVDEGADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENR 478
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   479 IKELEEELKRVKSEAIIARREPKEEAEDVSSYlctesdkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmi 558
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWKLEQLAADLSKY----------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE-- 503

                          170
                   ....*....|....*..
gi 767987055   559 RASREHPSVQEKKKSTI 575
Cdd:TIGR02169  504 ERVRGGRAVEEVLKASI 520
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 39-239 1.72e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 46.10  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   39 EFERLIHCYDEEVVK---ELMPLVVNVLENLDSVLS--ENQEHEVELELLREDNEQLLTQYEREK----ALRRQAEEKFI 109
Cdd:COG5185   326 ELEESKRETETGIQNltaEIEQGQESLTENLEAIKEeiENIVGEVELSKSSEELDSFKDTIESTKesldEIPQNQRGYAQ 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  110 EFEDALEQEKKELQIQVEHY----EFQTRQLELKAKNYADQISRLEERESEMKKEYNA-LHQRHTEMIQTYVEHIERSKM 184
Cdd:COG5185   406 EILATLEDTLKAADRQIEELqrqiEQATSSNEEVSKLLNELISELNKVMREADEESQSrLEEAYDEINRSVRSKKEDLNE 485

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987055  185 ------QQVGGNSQTESSLPGRSPRQ--SWRKSRKERPTSLNVFPLADGTVRAQIGGKLVPAG 239
Cdd:COG5185   486 eltqieSRVSTLKATLEKLRAKLERQleGVRSKLDQVAESLKDFMRARGYAHILALENLIPAS 548
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-186 1.84e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4372    25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767987055  138 LKAKNYADQISRLEEREsemkKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   105 SLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 430-556 1.99e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   430 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 506
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987055   507 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 556
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
PRK12495 PRK12495
hypothetical protein; Provisional
 867-968 2.95e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 43.70  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  867 SRGDTPVLDKGQG-EVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATL-------RPGPLTEHVFTDPAPTPSSGP 938
Cdd:PRK12495   69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTsatdeaaTDPPATAAARDGPTPDPTAQP 148

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767987055  939 -QPGSENGPEPDSSSTRPEPEPSGDPTGAGS 968
Cdd:PRK12495  149 aTPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 866-973 3.83e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  866 SSRGDTPVLDKGQGEVATIAngkvnpSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENG 945
Cdd:PRK07764  400 SAAAAAPAAAPAPAAAAPAA------AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA 473

                          90       100
                  ....*....|....*....|....*...
gi 767987055  946 PEPdssSTRPEPEPSGDPTGAGSSAAPT 973
Cdd:PRK07764  474 PEP---TAAPAPAPPAAPAPAAAPAAPA 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-186 3.83e-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: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767987055  141 KNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 66-185 3.90e-04

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


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 44.17  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    66 LDSVLSENQEH--EVELELLREDNEQLLTQYEREKALRRQAE---EKFIEFEDALEQEKKElqiqvehyeFQTRQLELKa 140
Cdd:pfam09728  172 LQQATEEEEKKaqEKEVAKARELKAQVQTLSETEKELREQLNlyvEKFEEFQDTLNKSNEV---------FTTFKKEME- 241

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 767987055   141 kNYADQISRLEERESEMKKEYNALHQRHTEMI---QTYVEHIERSKMQ 185
Cdd:pfam09728  242 -KMSKKIKKLEKENLTWKRKWEKSNKALLEMAeerQKLKEELEKLQKK 288
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-186 3.99e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   62 VLENLDSVLSENQEHEVELELLRED----NEQLLTQYEREKALRRQAEEKFIEFEDA------LEQEKKELQIQVEHYEF 131
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEEleqaRSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987055  132 QTRQLELKAKNYADQISRLEERESEMKKEYNALH------QRHTEMIQTYVEHIERSKMQQ 186
Cdd:COG4372   123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ 183
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 35-217 4.18e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    35 SIYREFERLIHCYDEevVKELMPLVVNVLENL-----------DSVLSENQEHEVELELlrEDNEQLLTQYEREKALRRQ 103
Cdd:TIGR00618  567 EIQQSFSILTQCDNR--SKEDIPNLQNITVRLqdlteklseaeDMLACEQHALLRKLQP--EQDLQDVRLHLQQCSQELA 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   104 AEEKfiefedALEQEKKEL-QIQVEHYEFQTRQLELKAKnyadQISRLEERESEMKKEYNA-----LHQRHTEM--IQTY 175
Cdd:TIGR00618  643 LKLT------ALHALQLTLtQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTywkemLAQCQTLLreLETH 712

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 767987055   176 VEHIERSKMQQVGGNSQTESSLPGR--SPRQSWRKSRKERPTSL 217
Cdd:TIGR00618  713 IEEYDREFNEIENASSSLGSDLAARedALNQSLKELMHQARTVL 756
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-170 4.43e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLELKAK- 141
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQl 402

                          90       100       110
                  ....*....|....*....|....*....|
gi 767987055  142 -NYADQISRLEERESEMKKEYNALHQRHTE 170
Cdd:COG1196   403 eELEEAEEALLERLERLEEELEELEEALAE 432
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 60-167 4.79e-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: 41.47  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    60 VNVLENLDSVLSENQEHEVELELLREDNE---QLLTQ----YERE--------KALRR------QAEEKFIEFEDALEQE 118
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaEIAREaqqnYERElvlhaediKALQAlreelnELKAEIAELKAEAESA 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 767987055   119 KKELQIQVEHYEFQTRQLElkaknyaDQISRLEERESEMKKEYNALHQR 167
Cdd:pfam07926   84 KAELEESEESWEEQKKELE-------KELSELEKRIEDLNEQNKLLHDQ 125
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-310 5.18e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEhevELELLREDNEQLltqyEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG3883   121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  143 YADQISRLEERESEMKKEYNALH--QRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRSPRQSWRKSRKERPTSLNVF 220
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  221 PLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNES 300
Cdd:COG3883   274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGG 353

                         250
                  ....*....|
gi 767987055  301 LQPLGDYGVG 310
Cdd:COG3883   354 GGGGSSSGGG 363
PRK12704 PRK12704
phosphodiesterase; Provisional
 72-152 5.83e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   72 ENQEHEVELELlREDNEQLLTQYEREKALRR----QAEEKFIEFE-------DALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:PRK12704   52 EAIKKEALLEA-KEEIHKLRNEFEKELRERRnelqKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKE 130

                          90
                  ....*....|....*.
gi 767987055  141 KNY----ADQISRLEE 152
Cdd:PRK12704  131 EELeeliEEQLQELER 146
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 861-975 6.72e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  861 PRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQP 940
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARE 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767987055  941 GSengPEPDSSSTRPEPEPSGDPTGAGSSAAPTMW 975
Cdd:PHA03307  104 GS---PTPPGPSSPDPPPPTPPPASPPPSPAPDLS 135
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-183 6.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   74 QEHEVELELLREDNEQLLTQYEREKALRRQAEE--KFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLE 151
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767987055  152 ERE---SEMKKEYNALHQRHT--EMIQTYVEHIERSK 183
Cdd:PRK03918  342 ELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-183 7.99e-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: 43.37  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    72 ENQEHEVELELLREDNEQL----LTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQV--EHYEFQTRQLELKAKNyad 145
Cdd:pfam13868   70 ERKRYRQELEEQIEEREQKrqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE--- 146

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767987055   146 qisRLEERESEMK-KEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  147 ---KEEEREEDERiLEYLKEKAEREEEREAEREEIEEEK 182
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 67-194 8.80e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   67 DSVLSEN-QEHEVELE-LLREDneQLLTQYEREKALRRQAEEkfiefedALEQEKKELQiqvEHYEFQTRQLELKAKNYA 144
Cdd:cd16269   169 EEVLQEFlQSKEAEAEaILQAD--QALTEKEKEIEAERAKAE-------AAEQERKLLE---EQQRELEQKLEDQERSYE 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767987055  145 DQISRLEEresEMKKEYNALHQRHTEMIQTYVEHIERskMQQVGGNSQTE 194
Cdd:cd16269   237 EHLRQLKE---KMEEERENLLKEQERALESKLKEQEA--LLEEGFKEQAE 281
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 445-525 1.04e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  445 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 514
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596

                          90
                  ....*....|.
gi 767987055  515 SDKIPMAQRRR 525
Cdd:PRK00409  597 QKGGYASVKAH 607
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 39-160 1.10e-03

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


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.22  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   39 EFERLIHCYDEEVVKELMPLVVNVLENLdsvLSENQEhevelelLREDNEQL---LTQY-EREKALRR---QAEEkfiEF 111
Cdd:COG3599    12 EFKKGFRGYDEDEVDEFLDEVAEDYERL---IRENKE-------LKEKLEELeeeLEEYrELEETLQKtlvVAQE---TA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767987055  112 EDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEEresEMKKE 160
Cdd:COG3599    79 EEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREIE---ELKRQ 124
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-179 1.23e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL----KAKNYADQISRLEERESEMKKEY 161
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereeKEQELQKKEQELQQLQQKAQQEL 85

                           90
                   ....*....|....*...
gi 767987055   162 NALHQRHTEMIQTYVEHI 179
Cdd:pfam03938   86 QKKQQELLQPIQDKINKA 103
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 72-186 1.26e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    72 ENQEHEVElELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQeKKELQIQVEHYEfQTRQLE----LKAKNYADQI 147
Cdd:pfam13868   30 EKKRIKAE-EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIEERE-QKRQEEyeekLQEREQMDEI 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 767987055   148 SRLEERESEMKKEYNALHQRHT--EMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  107 VERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEK 147
GreA_GreB_N pfam03449
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
 463-490 1.28e-03

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


Pssm-ID: 460920 [Multi-domain]  Cd Length: 71  Bit Score: 38.51  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....*...
gi 767987055   463 GELEAAKQAKVKLENRIKELEEELKRVK 490
Cdd:pfam03449   43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 444-564 1.38e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.90  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   444 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 520
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767987055   521 AQRRRFTRVEMARVLMERNQYKERLMELQEavrwtEMIRASREH 564
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVERKEEEARRLQE-----ELEEAREEE 120
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 63-168 1.51e-03

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


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 41.35  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRR----QAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLEL 138
Cdd:pfam06785   85 FKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQiqlqQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRS 164

                           90       100       110
                   ....*....|....*....|....*....|
gi 767987055   139 KAKNYADQISRLEERESEMKKEYNALHQRH 168
Cdd:pfam06785  165 VLEKRQDQIENLESKVRDLNYEIKTLLQLA 194
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 41-573 1.55e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    41 ERLIHCYDEEVvKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQY----EREKALRRQAEE---KFIEFED 113
Cdd:TIGR02169  307 ERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEvdkEFAETRD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   114 ALEQEKKEL-QIQVEHYEFQTRQLELKaknyaDQISRLEERESEMKKEYNALHQRHTEM------IQTYVEHIERSKMQQ 186
Cdd:TIGR02169  386 ELKDYREKLeKLKREINELKRELDRLQ-----EELQRLSEELADLNAAIAGIEAKINELeeekedKALEIKKQEWKLEQL 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   187 VGGNSQTESSLpgRSPRQSWRKSRKERPTSLNVFPLADGTVRAqiggklvpagdhwhlsdlgqLQSSSSYQCPQDEMSES 266
Cdd:TIGR02169  461 AADLSKYEQEL--YDLKEEYDRVEKELSKLQRELAEAEAQARA--------------------SEERVRGGRAVEEVLKA 518

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   267 GQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLqpLGDYGVGSKNSKRAREKRDSR------NmevQVTQEMRNVSIG 340
Cdd:TIGR02169  519 SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVV--VEDDAVAKEAIELLKRRKAGRatflplN---KMRDERRDLSIL 593

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   341 mgSSDEWSDVQ-DIIDSTPELdmcpetrldrtgssptQGIVNKAFGintDSLyhelstagseVIGDVDEGADLLGEFSgM 419
Cdd:TIGR02169  594 --SEDGVIGFAvDLVEFDPKY----------------EPAFKYVFG---DTL----------VVEDIEAARRLMGKYR-M 641

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   420 GKEVGNLLlENSQLL----ETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRV--KSEA 493
Cdd:TIGR02169  642 VTLEGELF-EKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrKIGE 720

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   494 IIARREP--------KEEAEDVSSYLCTESDKIPMAQRrrftrvEMARVLMERNQYKERLMELQEAVrwtEMIRASREHP 565
Cdd:TIGR02169  721 IEKEIEQleqeeeklKERLEELEEDLSSLEQEIENVKS------ELKELEARIEELEEDLHKLEEAL---NDLEARLSHS 791


                   ....*...
gi 767987055   566 SVQEKKKS 573
Cdd:TIGR02169  792 RIPEIQAE 799
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 891-973 1.69e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  891 PSQSTEEATEATEVPDPGPSEPETATLRPGPltehVFTDPAPTPSSGPQP--GSENGPEPDSSSTRPEPEPSGDPTGAGS 968
Cdd:PRK07764  396 AAAPSAAAAAPAAAPAPAAAAPAAAAAPAPA----AAPQPAPAPAPAPAPpsPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471


                  ....*
gi 767987055  969 SAAPT 973
Cdd:PRK07764  472 AAPEP 476
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 76-171 1.73e-03

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


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 40.24  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    76 HEVELELLREDNEQLLTQYEREKALRRQAEEKFI---------EFEDALEQEKKELQIQVEhyefqtrqlelkaknyadQ 146
Cdd:pfam12474   23 YEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIraeqkkrlkMFRESLKQEKKELKQEVE------------------K 84

                           90       100
                   ....*....|....*....|....*.
gi 767987055   147 ISRLEERESE-MKKEYNALHQRHTEM 171
Cdd:pfam12474   85 LPKFQRKEAKrQRKEELELEQKHEEL 110
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 71-212 1.75e-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: 42.85  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    71 SENQEHEVELELLREDNEQLLTQYERekalRRQAEEkfiEFEDALEQEKKELQIQVEHYEFQ------TRQ--------L 136
Cdd:pfam01576   57 AEAEEMRARLAARKQELEEILHELES----RLEEEE---ERSQQLQNEKKKMQQHIQDLEEQldeeeaARQklqlekvtT 129

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767987055   137 ELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQ--TESSLPGRSPRQSwrKSRKE 212
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeaMISDLEERLKKEE--KGRQE 205
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 63-187 2.01e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.52  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEHEVELEL--LREDNEQLLTQ----Y---EREKALRRQAEEKFIEFEDALE---QEKKELQIQVEH-- 128
Cdd:PRK04778  258 IQDLKEQIDENLALLEELDLdeAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEhakEQNKELKEEIDRvk 337

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987055  129 --YEFQTRQLElKAKNYADQISRLEERESEMKKEYNALHQRHT---EMIQTYVEHIERSKMQQV 187
Cdd:PRK04778  338 qsYTLNESELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSelqEELEEILKQLEEIEKEQE 400
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-166 2.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALE-----QEKKELQIQVEHYEFQTRQLE 137
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELE 152

                          90       100
                  ....*....|....*....|....*....
gi 767987055  138 LKAKNYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEE 181
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-186 2.09e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEkfiefedaLEQEKKELQIQVEHYEFQTRQLELKA-K 141
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE--------LEAELAELQEELEELLEQLSLATEEElQ 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767987055  142 NYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIERSKMQQ 186
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAA 239
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 445-492 2.13e-03

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


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 39.50  E-value: 2.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767987055   445 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSE 492
Cdd:pfam17675   44 EELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEE 91
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 53-179 2.25e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 40.16  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   53 KELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQ--YEREKALR--RQAEEKFIefEDALEQEKKELQIQVEH 128
Cdd:PRK14471   31 KPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEarAERDAILKeaREIKEKMI--ADAKEEAQVEGDKMIEQ 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767987055  129 YEfQTRQLELKA-----KNYADQISrLEERESEMKKEYNALHQRHtEMIQTYVEHI 179
Cdd:PRK14471  109 AK-ASIESEKNAamaeiKNQVANLS-VEIAEKVLRKELSNKEKQH-KLVEKMLGDV 161
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
 390-494 2.51e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153284 [Multi-domain]  Cd Length: 242  Bit Score: 41.19  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  390 SLYHELS---TAGSEVIG-----DVDEGADLLGEFSGMGKEVGNLLLENSQLLETK-NA-LNVVKNDLIAKVDQLSGEQE 459
Cdd:cd07600    78 TLNHALSraaLASSLELKslepeDEDPLSKALGKYSDAEEKIAEARLEQDQLIQKEfNAkLRETLNTSFQKAHKARKKVE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767987055  460 VLRGELEAAKQAKVKLENRIKE---------LEEELKRVKSEAI 494
Cdd:cd07600   158 DKRLQLDTARAELKSAEPAEKQeaarvevetAEDEFVSATEEAV 201
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
430-572 2.51e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  430 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 506
Cdd:COG4372    93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987055  507 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 572
Cdd:COG4372   169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 63-186 2.52e-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: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    63 LENLDSVLS----------------ENQEHEVElELLREDNEQLLT------QYEREKA-LRRQAEEKfiefedalEQEK 119
Cdd:pfam01576  442 LESVSSLLNeaegkniklskdvsslESQLQDTQ-ELLQEETRQKLNlstrlrQLEDERNsLQEQLEEE--------EEAK 512

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767987055   120 KELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYvEHIERSK--MQQ 186
Cdd:pfam01576  513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY-DKLEKTKnrLQQ 580
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 50-163 2.59e-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: 41.67  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   50 EVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhy 129
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-- 216

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767987055  130 efqtrQLELKAKNYADQISRLEERESEMKKEYNA 163
Cdd:COG4942   217 -----ELQQEAEELEALIARLEAEAAAAAERTPA 245
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 89-213 2.64e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    89 QLLTQYEREKAL-RRQAEEKFIEFE-DALEQEKKELQIQVEHY----EFQT-RQLEL--KAKNYADQISRLEERESEMKK 159
Cdd:pfam17380  273 QLLHIVQHQKAVsERQQQEKFEKMEqERLRQEKEEKAREVERRrkleEAEKaRQAEMdrQAAIYAEQERMAMERERELER 352

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767987055   160 EYNALHQRHTEMIQTYVEHIERSKMQQVgGNSQTESSLPGRSPRQSWRKSRKER 213
Cdd:pfam17380  353 IRQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVK 405
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 103-186 2.66e-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: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   103 QAEEKFIEFEDAL-EQEKKELQIQVEHYEFQTRQLElKAKNYADQ-ISRLEERESEMKKEYNALHQRHTEM--IQTYVEH 178
Cdd:pfam10368   15 ELEKPFEEQQEPLvELEKKEQELYEEIIELGMDEFD-EIKKLSDEaLENVEEREELLEKEKESIEEAKEEFkkIKEIIEE 93


                   ....*...
gi 767987055   179 IERSKMQQ 186
Cdd:pfam10368   94 IEDEELKK 101
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 74-183 2.71e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    74 QEHEVELELLREDNEQLL----TQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISR 149
Cdd:pfam13868   87 QKRQEEYEEKLQEREQMDeiveRIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166

                           90       100       110
                   ....*....|....*....|....*....|....
gi 767987055   150 LEERESEMKKEYNALHQRHTEMIQTYVEHIERSK 183
Cdd:pfam13868  167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 61-186 2.73e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    61 NVLENLDSVLSENQEHEVELELLREDNEQLLTQYERE-KALRRQAeekfiefeDALEQEKKELQI-------QVEHYEFQ 132
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREAL--------DELRAELTLLNEeaanlreRLESLERR 832

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767987055   133 TRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEH-IERSKMQQ 186
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEE 887
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 74-164 2.77e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   74 QEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELqiqvehyefqtRQLELKAKNYADQISRLEER 153
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-----------KRLELEIEEVEARIKKYEEQ 81

                          90
                  ....*....|...
gi 767987055  154 ESEMK--KEYNAL 164
Cdd:COG1579    82 LGNVRnnKEYEAL 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 389-574 3.21e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   389 DSLYHELSTAGSEVIGDVDEGADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAA 468
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   469 KQAKVKLENRIK--------------ELEEELKRVKSEAIIARREPKEEAEDVSSylcTESDKIPMAQRRRFTRVEMARV 534
Cdd:TIGR02168  781 EAEIEELEAQIEqlkeelkalrealdELRAELTLLNEEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESL 857

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767987055   535 LMERNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 574
Cdd:TIGR02168  858 AAEIEELEELIEELESELeALLNERASLEEALALLRSELEE 898
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 64-165 3.32e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   64 ENLDSVL--SENQEHEVE-----LELLREDNEQLLTQY--------EREKALRRQAEEkfiEFEDALEQEKKE------- 121
Cdd:PRK00409  516 EKLNELIasLEELERELEqkaeeAEALLKEAEKLKEELeekkeklqEEEDKLLEEAEK---EAQQAIKEAKKEadeiike 592

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767987055  122 --LQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALH 165
Cdd:PRK00409  593 lrQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-171 3.32e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   72 ENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADqISRLE 151
Cdd:COG1196   688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELE 766

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767987055  152 ERESEMKK--------------EYNALHQRHTEM 171
Cdd:COG1196   767 RELERLEReiealgpvnllaieEYEELEERYDFL 800
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 73-186 3.56e-03

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


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 41.86  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    73 NQEHEVELELLREDNEQLltqyEREKALRRqaeekfiefEDALEQEKKELQIQVEHyefqtrqlELKAKNYADQISRLEE 152
Cdd:pfam15818  273 NTEMEAELKALKENNQTL----ERDNELQR---------EKVKENEEKFLNLQNEH--------EKALGTWKKHVEELNG 331

                           90       100       110
                   ....*....|....*....|....*....|....
gi 767987055   153 RESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQ 186
Cdd:pfam15818  332 EINEIKNELSSLKETHIKLQEHYNKLCNQKKFEE 365
Filament pfam00038
Intermediate filament protein;
410-563 3.64e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.06  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   410 ADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---L 486
Cdd:pfam00038   57 EDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEElafL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   487 KRVKSEAIiarREPKEEAEDVSSYLctESDKIPmaqrrrftRVEMARVLME-RNQYKE---------------RLMELQE 550
Cdd:pfam00038  137 KKNHEEEV---RELQAQVSDTQVNV--EMDAAR--------KLDLTSALAEiRAQYEEiaaknreeaeewyqsKLEELQQ 203

                          170
                   ....*....|....
gi 767987055   551 AV-RWTEMIRASRE 563
Cdd:pfam00038  204 AAaRNGDALRSAKE 217
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 458-506 3.82e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.39  E-value: 3.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767987055  458 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 506
Cdd:COG0711    33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
445-563 3.97e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  445 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSylctesdkipmaqrr 524
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE--------------- 112

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767987055  525 rfTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 563
Cdd:COG4372   113 --LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 59-174 4.04e-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: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   59 VVNVLENLDSVLSENQEHEVELELLRE----DNEQL--------LTQYERE----KALRRQAEEKFIEFEDALEQEKKEL 122
Cdd:COG1579    47 LEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLgnvrnnkeYEALQKEieslKRRISDLEDEILELMERIEELEEEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767987055  123 QiQVEhyefqtRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQT 174
Cdd:COG1579   127 A-ELE------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 900-971 4.35e-03

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 41.14  E-value: 4.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767987055  900 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 971
Cdd:NF041121   17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
445-505 4.35e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 4.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987055  445 NDLIAKVDQLSGEQEVLRGELEaakqakvKLENRIKELEEELKRVKSEaiiARREPKEEAE 505
Cdd:COG2433   416 RRLEEQVERLEAEVEELEAELE-------EKDERIERLERELSEARSE---ERREIRKDRE 466
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 458-506 4.77e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 4.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767987055  458 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 506
Cdd:cd06503    32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 72-170 4.78e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.36  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    72 ENQEHEVELELLRED----NEQLLTQYEREKAL---RRQAEEKFIEFE---DALEQEKKELQIQVEHYEFQTRQLELKAK 141
Cdd:pfam20492    7 EKQELEERLKQYEEEtkkaQEELEESEETAEELeeeRRQAEEEAERLEqkrQEAEEEKERLEESAEMEAEEKEQLEAELA 86

                           90       100       110
                   ....*....|....*....|....*....|....
gi 767987055   142 NYADQISRLEE----RESEMKK-EYNALHQRHTE 170
Cdd:pfam20492   87 EAQEEIARLEEeverKEEEARRlQEELEEAREEE 120
PRK12704 PRK12704
phosphodiesterase; Provisional
 74-173 5.54e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   74 QEHEVELELLREdnEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEER 153
Cdd:PRK12704   45 EEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                          90       100
                  ....*....|....*....|
gi 767987055  154 ESEMKKEYNALHQRHTEMIQ 173
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQ 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-181 5.61e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767987055  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 83-210 5.73e-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: 40.52  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   83 LREDNEQLLTQYEREKALRRQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYN 162
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767987055  163 ALHQRHTEMIQTyvehierskMQQVGGNSQTESSLPGRSPRQSWRKSR 210
Cdd:COG4942   101 AQKEELAELLRA---------LYRLGRQPPLALLLSPEDFLDAVRRLQ 139
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 79-159 6.17e-03

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


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 39.29  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    79 ELELLREDNEQLLTQYEREKAL------------RRQAEEK----FIEFEDALEQEKKelqiQVEHY--EFQTRQLELKA 140
Cdd:pfam05300   60 EEELRKKIKEELYKRLEQEQAKvqeelarlaereREAAQESltraILRERASTEDERL----KAQQLakQLEEKEAELKK 135

                           90       100
                   ....*....|....*....|.
gi 767987055   141 KN--YADQISRLEERESEMKK 159
Cdd:pfam05300  136 QDafYKEQLARLEEKNAEFYK 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-181 6.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   63 LENLDSVLSENQEhevELELLREDNEQLLTQYEREKALRRQAEEKfiefEDALEQEKKELQIQVEHYEFQTRQLELKAKN 142
Cdd:COG1196   276 LEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEE 348

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767987055  143 YADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-181 7.23e-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: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   64 ENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFED---ALEQEKKELQIQVEHYEFQTRQLELKA 140
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEELEEAEEELEEAEAELAEAEEAL 367

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767987055  141 KNYADQISRLEERESEMKKEYNALHQRHTEmIQTYVEHIER 181
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEE 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-183 7.40e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    33 AGSIYREFERLIHCYDEEVVkELMPLVVNVLENLDSVLSENQEH-------EVELELLREDNEQLLTQYEREKALRRQAE 105
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALaneisrlEQQKQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   106 EKFIEFED---ALEQEKKELQIQVE-------HYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRhtemIQTY 175
Cdd:TIGR02168  330 SKLDELAEelaELEEKLEELKEELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERL 405


                   ....*...
gi 767987055   176 VEHIERSK 183
Cdd:TIGR02168  406 EARLERLE 413
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-186 7.86e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   65 NLDSVLSENQEHEVELELLREDN---EQLLTQYEREKALRRQAEEKFIEFEDALEQEKKEL-QIQVEHYEFQTRQLELKA 140
Cdd:COG4913   662 DVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAED 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767987055  141 KNYADQISRLEER---------ESEMKKEYNALHQRHTEMIQTYVEHIERsKMQQ 186
Cdd:COG4913   742 LARLELRALLEERfaaalgdavERELRENLEERIDALRARLNRAEEELER-AMRA 795
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 431-552 7.93e-03

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


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 37.76  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   431 SQLLETKNALNVVKNDLIAKVDQLSgEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAiiarREPKEEAEDVSSY 510
Cdd:pfam04871    8 SEASSLKNENTELKAELQELSKQYN-SLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKE----KEKQSELDDLLLL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767987055   511 LCTESDKipmaqrrrftrvemarvlmeRNQYKERLMELQEAV 552
Cdd:pfam04871   83 LGDLEEK--------------------VEKYKARLKELGEEV 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 426-551 7.94e-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: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055  426 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARrepkeeae 505
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LAR-------- 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767987055  506 dvssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 551
Cdd:COG1196   300 -------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-166 8.28e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   72 ENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKEL--------QIQVEHYEFQTRQLEL--KAK 141
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaeaelaEAEEELEELAEELLEAlrAAA 396

                          90       100
                  ....*....|....*....|....*
gi 767987055  142 NYADQISRLEERESEMKKEYNALHQ 166
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEE 421
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 77-186 9.16e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055    77 EVELELLREDNEQLLtQYEREKALR---------RQAEEKFIEFEDALEQEKKELQIQVEHYefqtrqlELKAKNYADQI 147
Cdd:pfam13868  144 ELEKEEEREEDERIL-EYLKEKAEReeereaereEIEEEKEREIARLRAQQEKAQDEKAERD-------ELRAKLYQEEQ 215

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767987055   148 SRlEERESEMKKEYNALHQRHtEMIQTYVEHIERSKMQQ 186
Cdd:pfam13868  216 ER-KERQKEREEAEKKARQRQ-ELQQAREEQIELKERRL 252
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 86-188 9.27e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 9.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055     86 DNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEhyEFQTRQLELKAKNYADQISRLEERESEMKKEYNA-- 163
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKE--KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKlq 82

                            90       100
                    ....*....|....*....|....*..
gi 767987055    164 --LHQRHTEMIQTYVEHIERSkMQQVG 188
Cdd:smart00935   83 qdLQKRQQEELQKILDKINKA-IKEVA 108
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-181 9.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987055   58 LVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFE-DALEQEKKELQIQVEHYEFQTRQL 136
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERERRRARLEALLAAL 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767987055  137 ELK----AKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIER 181
Cdd:COG4913   372 GLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
 
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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