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Conserved domains on  [gi|2462548076|ref|XP_054235846|]
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C-Jun-amino-terminal kinase-interacting protein 3 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 694-918 1.29e-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: 177.90  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  694 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 771
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  772 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 851
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548076  852 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 918
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 163-231 1.77e-31

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: 117.41  E-value: 1.77e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548076  163 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 231
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
Trypan_PARP super family cl42451
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 589-703 2.21e-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.


The actual alignment was detected with superfamily member pfam05887:

Pssm-ID: 368653  Cd Length: 134  Bit Score: 56.72  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  589 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 665
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462548076  666 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 703
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 188-308 1.02e-05

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: 45.68  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  188 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 264
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462548076  265 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 308
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 694-918 1.29e-47

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 177.90  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  694 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 771
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  772 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 851
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548076  852 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 918
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 163-231 1.77e-31

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: 117.41  E-value: 1.77e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548076  163 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 231
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 589-703 2.21e-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: 56.72  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  589 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 665
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462548076  666 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 703
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 188-308 1.02e-05

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: 45.68  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  188 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 264
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462548076  265 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 308
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-300 4.46e-05

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: 47.74  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  174 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 250
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548076  251 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 300
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
792-914 4.59e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  792 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 864
Cdd:COG3292    265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462548076  865 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 914
Cdd:COG3292    343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK11633 PRK11633
cell division protein DedD; Provisional
 635-722 9.37e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 44.99  E-value: 9.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  635 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 709
Cdd:PRK11633    64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143

                           90
                   ....*....|...
gi 2462548076  710 AGSSAAPTMWLGA 722
Cdd:PRK11633   144 APTGKAYVVQLGA 156
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
174-316 1.42e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  174 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 250
Cdd:COG4372     93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548076  251 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 316
Cdd:COG4372    169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 189-269 7.91e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  189 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 258
Cdd:PRK00409   519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596

                           90
                   ....*....|.
gi 2462548076  259 SDKIPMAQRRR 269
Cdd:PRK00409   597 QKGGYASVKAH 607
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 202-250 1.95e-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: 39.77  E-value: 1.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548076  202 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 250
Cdd:COG0711     33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-294 2.87e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  166 EVGNLLLE--NSQLLETKNALNvvknDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARRE 243
Cdd:TIGR02169  857 ENLNGKKEelEEELEELEAALR----DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548076  244 PKE----EAEDVSSYLCTESDKIPMAQRRRFTR-------VEM------ARVLMERNQYKERLMELQE 294
Cdd:TIGR02169  933 LSEiedpKGEDEEIPEEELSLEDVQAELQRVEEeiralepVNMlaiqeyEEVLKRLDELKEKRAKLEE 1000
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
166-319 3.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  166 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---RGELEAAK-------QAKVKLENRIKELEEELK 231
Cdd:PRK03918   190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  232 RVKSEAiiarREPKEEAEDVssylctESDKiPMAQRRRftrvemaRVLMERNQYKERLMELQ-EAVRWTEMIRASREHPS 310
Cdd:PRK03918   270 ELKKEI----EELEEKVKEL------KELK-EKAEEYI-------KLSEFYEEYLDELREIEkRLSRLEEEINGIEERIK 331


                   ....*....
gi 2462548076  311 VQEKKKSTI 319
Cdd:PRK03918   332 ELEEKEERL 340
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 202-250 3.77e-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: 3.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548076  202 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 250
Cdd:cd06503     32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 644-715 5.03e-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: 40.76  E-value: 5.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548076  644 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 715
Cdd:NF041121    17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 694-918 1.29e-47

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 177.90  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  694 SSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCL--HSIKLKDSVLSLVHVKGRVLVALADGTLAIF 771
Cdd:pfam19056   80 PEEPEPEEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  772 HRGEDGQWDLSNYHLMDLGHphHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVS 851
Cdd:pfam19056  160 ARAEDGLWDPEPPKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548076  852 IRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGtgklGFSFVRITALLVAGSRLWVGTGNGVVISIPL 918
Cdd:pfam19056  238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 163-231 1.77e-31

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: 117.41  E-value: 1.77e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462548076  163 MGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELK 231
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 589-703 2.21e-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: 56.72  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  589 VLAGitlVGCATRCNVPRSNCSSRGDtpvldKGQGEVATIANGKVN---PSQSTEEATEATEVPDPGPsEPEtatlrPGP 665
Cdd:pfam05887   18 LFAG---VGFAAAAEGPEDKGLTKGG-----KGKGKGTKVSDDDTNgtdPEPEPEPEPEPEPEPEPEP-EPE-----PEP 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462548076  666 ltehvftDPAPTPSSGPQPGSENGPEPDsssTRPEPEP 703
Cdd:pfam05887   84 -------EPEPEPEPEPEPEPEPEPEPE---PEPEPEP 111
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 188-308 1.02e-05

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: 45.68  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  188 KNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAIIARREPKEEAEDvssylcTESDKIPM 264
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEESAEM------EAEEKEQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462548076  265 AQRRRFTRVEMARVLMERNQyKErlmelQEAVRW-TEMIRASREH 308
Cdd:pfam20492   82 EAELAEAQEEIARLEEEVER-KE-----EEARRLqEELEEAREEE 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-300 4.46e-05

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: 47.74  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  174 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAED 250
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462548076  251 VSSYlcteSDKIPMAQRRR-------------FTRVEMARVLMERNQYKERLMELQEAVRWTE 300
Cdd:TIGR02168  402 IERL----EARLERLEDRRerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLE 460
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
792-914 4.59e-05

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 47.68  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  792 PHHSIRCMAVVYD-----RVWCG-YKNKVHVIQPKTMQIeKSFDAHPRRESQVRQLAWIGDG-VWVSIRlDSTLRLYHAH 864
Cdd:COG3292    265 SGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYDPK 342

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462548076  865 THQhlqdvdIEPYvskmlgTGKLGFSFVRITALLVAGS-RLWVGTGNGVVI 914
Cdd:COG3292    343 TGK------FTKF------SEDNGLSNNFIRSILEDSDgNLWVGTNGGLYR 381
PRK11633 PRK11633
cell division protein DedD; Provisional
 635-722 9.37e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 44.99  E-value: 9.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  635 PSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSST-----RPEPEPSGDPTG 709
Cdd:PRK11633    64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEappapKPEPKPVVEEKA 143

                           90
                   ....*....|...
gi 2462548076  710 AGSSAAPTMWLGA 722
Cdd:PRK11633   144 APTGKAYVVQLGA 156
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
174-316 1.42e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  174 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPKEEAed 250
Cdd:COG4372     93 QAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAA-- 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548076  251 vssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKK 316
Cdd:COG4372    169 ------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
Filament pfam00038
Intermediate filament protein;
170-307 2.20e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 44.53  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  170 LLLENSQL-LETKNALNVVKnDLIAKV-DQLSGEQEV------LRGELEAAKQAKVKLENRIKELEEE---LKRVKSEAI 238
Cdd:pfam00038   66 LTVERARLqLELDNLRLAAE-DFRQKYeDELNLRTSAendlvgLRKDLDEATLARVDLEAKIESLKEElafLKKNHEEEV 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  239 iarREPKEEAEDVSSYLctESDKIPmaqrrrftRVEMARVLME-RNQYKE---------------RLMELQEAV-RWTEM 301
Cdd:pfam00038  145 ---RELQAQVSDTQVNV--EMDAAR--------KLDLTSALAEiRAQYEEiaaknreeaeewyqsKLEELQQAAaRNGDA 211


                   ....*.
gi 2462548076  302 IRASRE 307
Cdd:pfam00038  212 LRSAKE 217
PRK12495 PRK12495
hypothetical protein; Provisional
 611-712 2.49e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 43.70  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  611 SRGDTPVLDKGQG-EVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATL-------RPGPLTEHVFTDPAPTPSSGP 682
Cdd:PRK12495    69 TEDGAAGDDAGDGaEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTsatdeaaTDPPATAAARDGPTPDPTAQP 148

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462548076  683 -QPGSENGPEPDSSSTRPEPEPSGDPTGAGS 712
Cdd:PRK12495   149 aTPDERRSPRQRPPVSGEPPTPSTPDAHVAG 179
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
189-307 3.00e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  189 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARrepkEEAEDVSsylctesdkipmaQRR 268
Cdd:COG4372     48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----EELESLQ-------------EEA 110

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462548076  269 RFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 307
Cdd:COG4372    111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 175-296 3.69e-04

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: 41.23  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  175 SQLLETKNALNVVKNDLIAKVDQLSgEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAiiarREPKEEAEDVSSY 254
Cdd:pfam04871    8 SEASSLKNENTELKAELQELSKQYN-SLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKE----KEKQSELDDLLLL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462548076  255 LCTESDKipmaqrrrftrvemarvlmeRNQYKERLMELQEAV 296
Cdd:pfam04871   83 LGDLEEK--------------------VEKYKARLKELGEEV 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 173-319 4.20e-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: 44.67  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  173 ENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVS 252
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548076  253 SYlctesdkipmAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASREHPSVQEKKKSTI 319
Cdd:TIGR02169  466 KY----------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE--ERVRGGRAVEEVLKASI 520
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 189-236 4.26e-04

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: 41.43  E-value: 4.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462548076  189 NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSE 236
Cdd:pfam17675   44 EELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEE 91
GreA_GreB_N pfam03449
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure.
 207-234 4.31e-04

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


Pssm-ID: 460920 [Multi-domain]  Cd Length: 71  Bit Score: 39.67  E-value: 4.31e-04
                           10        20
                   ....*....|....*....|....*...
gi 2462548076  207 GELEAAKQAKVKLENRIKELEEELKRVK 234
Cdd:pfam03449   43 AEYDAAKEEQAFIEARIRELEDKLANAE 70
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 193-317 4.90e-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: 44.29  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  193 AKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRV--KSEAIIARREP--------KEEAEDVSSYLCTESDKI 262
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrKIGEIEKEIEQleqeeeklKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462548076  263 PMAQRrrftrvEMARVLMERNQYKERLMELQEAVrwtEMIRASREHPSVQEKKKS 317
Cdd:TIGR02169  754 ENVKS------ELKELEARIEELEEDLHKLEEAL---NDLEARLSHSRIPEIQAE 799
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 610-717 4.94e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 4.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  610 SSRGDTPVLDKGQGEVATIAngkvnpSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENG 689
Cdd:PRK07764   400 SAAAAAPAAAPAPAAAAPAA------AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA 473

                           90       100
                   ....*....|....*....|....*...
gi 2462548076  690 PEPdssSTRPEPEPSGDPTGAGSSAAPT 717
Cdd:PRK07764   474 PEP---TAAPAPAPPAAPAPAAAPAAPA 498
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 201-307 6.55e-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: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  201 EQEVLRGELEAAK--QAKVKLENRIKELEEELKRV--------KSEAIIA-RREPKEEAEDVSSYLcteSDKIPMAQRRR 269
Cdd:pfam13868  124 KQRQLREEIDEFNeeQAEWKELEKEEEREEDERILeylkekaeREEEREAeREEIEEEKEREIARL---RAQQEKAQDEK 200

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462548076  270 FTRVEM-ARVLMERNQYKERLMELQEA---VRWTEMIRASRE 307
Cdd:pfam13868  201 AERDELrAKLYQEEQERKERQKEREEAekkARQRQELQQARE 242
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 189-269 7.91e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  189 NDLIAKVDQLSGEQEVLRGELEAAKQA----KVKLENRIKELEEELKRVKSEA------IIArrEPKEEAEDVSSYLCTE 258
Cdd:PRK00409   519 NELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAekeaqqAIK--EAKKEADEIIKELRQL 596

                           90
                   ....*....|.
gi 2462548076  259 SDKIPMAQRRR 269
Cdd:PRK00409   597 QKGGYASVKAH 607
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-318 8.43e-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: 43.51  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  127 DSLYHELSTAGSEVIGDVDEGADLLGEFS-VRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSG---EQ 202
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  203 EVLRGELEA----AKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSylcTESDKIPMAQRRRFTRVEMARV 278
Cdd:TIGR02168  781 EAEIEELEAqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESL 857

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462548076  279 LMERNQYKERLMELQEAV-RWTEMIRASREHPSVQEKKKST 318
Cdd:TIGR02168  858 AAEIEELEELIEELESELeALLNERASLEEALALLRSELEE 898
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
175-316 1.18e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  175 SQLLETKNALNVVKNDLIAKVDQLSGEQEVL---RGELEAAKQAKVKLE-----------------NRIKELEEELKRVK 234
Cdd:COG1340     74 KELKEERDELNEKLNELREELDELRKELAELnkaGGSIDKLRKEIERLEwrqqtevlspeeekelvEKIKELEKELEKAK 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  235 SEaiiarREPKEEAEDVSsylcTESDKIpMAQRRRFTRvEMARVLMERNQYKERLMEL-QEAvrwtEMIRASRE--HPSV 311
Cdd:COG1340    154 KA-----LEKNEKLKELR----AELKEL-RKEAEEIHK-KIKELAEEAQELHEEMIELyKEA----DELRKEADelHKEI 218


                   ....*
gi 2462548076  312 QEKKK 316
Cdd:COG1340    219 VEAQE 223
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 605-719 1.24e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  605 PRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQP 684
Cdd:PHA03307    24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARE 103

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462548076  685 GSengPEPDSSSTRPEPEPSGDPTGAGSSAAPTMW 719
Cdd:PHA03307   104 GS---PTPPGPSSPDPPPPTPPPASPPPSPAPDLS 135
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 176-296 1.94e-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: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  176 QLLETK-NALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARREPK-------EE 247
Cdd:COG1579     13 QELDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--IKKYEEQlgnvrnnKE 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462548076  248 AEDVSSylctESDKIpmAQRRRFTRVEMARVLMERNQYKERLMELQEAV 296
Cdd:COG1579     91 YEALQK----EIESL--KRRISDLEDEILELMERIEELEEELAELEAEL 133
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 202-250 1.95e-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: 39.77  E-value: 1.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548076  202 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 250
Cdd:COG0711     33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAaeIIaeARKEAEAIAEE 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-295 2.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  170 LLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEaiIARrepkeeae 249
Cdd:COG1196    230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--LAR-------- 299

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462548076  250 dvssylcTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEA 295
Cdd:COG1196    300 -------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 635-717 2.15e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  635 PSQSTEEATEATEVPDPGPSEPETATLRPGPltehVFTDPAPTPSSGPQP--GSENGPEPDSSSTRPEPEPSGDPTGAGS 712
Cdd:PRK07764   396 AAAPSAAAAAPAAAPAPAAAAPAAAAAPAPA----AAPQPAPAPAPAPAPpsPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471


                   ....*
gi 2462548076  713 SAAPT 717
Cdd:PRK07764   472 AAPEP 476
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
189-249 2.15e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 2.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462548076  189 NDLIAKVDQLSGEQEVLRGELEaakqakvKLENRIKELEEELKRVKSEaiiARREPKEEAE 249
Cdd:COG2433    416 RRLEEQVERLEAEVEELEAELE-------EKDERIERLERELSEARSE---ERREIRKDRE 466
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
 181-247 2.71e-03

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


Pssm-ID: 463241  Cd Length: 134  Bit Score: 39.11  E-value: 2.71e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462548076  181 KNALNVVKNDLIAKVDQLsgeqEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREpKEE 247
Cdd:pfam11221   59 EATQRELARDLILKAQQI----EYLIDSLPGIGVSEEEQLQRIKELEEELREAEEERQEAVKE-KEE 120
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-294 2.87e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  166 EVGNLLLE--NSQLLETKNALNvvknDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARRE 243
Cdd:TIGR02169  857 ENLNGKKEelEEELEELEAALR----DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462548076  244 PKE----EAEDVSSYLCTESDKIPMAQRRRFTR-------VEM------ARVLMERNQYKERLMELQE 294
Cdd:TIGR02169  933 LSEiedpKGEDEEIPEEELSLEDVQAELQRVEEeiralepVNMlaiqeyEEVLKRLDELKEKRAKLEE 1000
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-248 2.90e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  155 SVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVK 234
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90
                   ....*....|....*.
gi 2462548076  235 SE--AIIARREPKEEA 248
Cdd:TIGR02169  758 SElkELEARIEELEED 773
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
166-319 3.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  166 EVGNLLLENSQLLETK----NALNVVKNDLIAKVDQLSGEQEVL---RGELEAAK-------QAKVKLENRIKELEEELK 231
Cdd:PRK03918   190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelKEEIEELEkelesleGSKRKLEEKIRELEERIE 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548076  232 RVKSEAiiarREPKEEAEDVssylctESDKiPMAQRRRftrvemaRVLMERNQYKERLMELQ-EAVRWTEMIRASREHPS 310
Cdd:PRK03918   270 ELKKEI----EELEEKVKEL------KELK-EKAEEYI-------KLSEFYEEYLDELREIEkRLSRLEEEINGIEERIK 331


                   ....*....
gi 2462548076  311 VQEKKKSTI 319
Cdd:PRK03918   332 ELEEKEERL 340
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 202-250 3.77e-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: 3.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462548076  202 QEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEA--II--ARREPKEEAED 250
Cdd:cd06503     32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqeIIeeARKEAEKIKEE 84
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 174-236 4.07e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 4.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462548076  174 NSQLLETKNALNVVK---NDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSE 236
Cdd:COG3883     22 QKELSELQAELEAAQaelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 191-236 4.16e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.86  E-value: 4.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462548076  191 LIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSE 236
Cdd:pfam06005    9 LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQE 54
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 644-715 5.03e-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: 40.76  E-value: 5.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462548076  644 EATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAA 715
Cdd:NF041121    17 RAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAA 88
 
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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