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Conserved domains on  [gi|18858189|ref|NP_572495|]
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chromatin assembly factor 1, p180 subunit [Drosophila melanogaster]

Protein Classification

UBX domain-containing protein; M56 family metallopeptidase( domain architecture ID 13280863)

UBX domain-containing protein similar to Schizosaccharomyces pombe protein C17C9.11c| M56 family metallopeptidase is an integral membrane metallopeptidase, containing a zinc-binding HEXXH motif; it allows bacteria to respond to presence of beta-lactam antibiotics by expression of beta-lactamases and penicillin-binding proteins; includes transmembrane proteins BlaR1 and MecR1; may also contain type IVB secretion system protein DotG/IcmE at the C-terminal end

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00121 super family cl31754
MAEBL; Provisional
131-603 4.85e-22

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 103.68  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   131 EDVIELDEDEADKEIEDQDQLVEAKSSKEVKLKPKKSEGKKGSPapiQIKLPLVNKRSKRRKSLKKSEEplETSTADVAK 210
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKKADAAKKKAEE--AKKAAEAAK 1349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   211 GDSESSDDIEIIAEELNPQKRQKVQTPREKSPE--NSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKK--EEPKTAEQ 286
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEE 1429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   287 NKKNDQATIDLFMGKKMETNKKDKPEVKTTAKDNKKdplIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDS 366
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   367 TTKSK---------KEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMIL 437
Cdd:PTZ00121 1507 EAKKKadeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   438 STSEANSSSSEHEMDADTDTAATDRPSAQKETRLNRKSL---PEVTGAPKGLTPKQQ---RLMEQRKKAREEKEQKLAEE 511
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAeekKKAEELKKAEEENKIKAAEE 1666
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   512 RRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKK 591
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
                         490
                  ....*....|..
gi 18858189   592 EQEREEAEQKKK 603
Cdd:PTZ00121 1747 EEAKKDEEEKKK 1758
CAF1A pfam12253
Chromatin assembly factor 1 subunit A; The CAF-1 or chromatin assembly factor-1 consists of ...
770-813 4.06e-19

Chromatin assembly factor 1 subunit A; The CAF-1 or chromatin assembly factor-1 consists of three subunits, and this is the first, or A. The A domain is uniquely required for the progression of S phase in mouse cells, independent of its ability to promote histone deposition but dependent on its ability to interact with HP1 - heterochromatin protein 1-rich heterochromatin domains next to centromeres that are crucial for chromosome segregation during mitosis. This HP1-CAF-1 interaction module functions as a built-in replication control for heterochromatin, which, like a control barrier, has an impact on S-phase progression in addition to DNA-based checkpoints.


:

Pssm-ID: 463507  Cd Length: 75  Bit Score: 82.55  E-value: 4.06e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 18858189    770 KYLHFADNRRPPYYGTWRKKSSSISARRPLAQDKVLFDYEVDSD 813
Cdd:pfam12253    1 KLLQFYEDVRPPYYGTWTKKSSVVGPRNPFAKDLLGLDYDYDSD 44
CAF1-p150_C2 super family cl21343
CAF1 complex subunit p150, region binding to CAF1-p60 at C-term; CAF1-p150_C2 is part of the ...
947-1127 4.40e-05

CAF1 complex subunit p150, region binding to CAF1-p60 at C-term; CAF1-p150_C2 is part of the binding region of the CAF1 complex p150 subunit to the p60 subunit. The CAF1 complex is essential in human cells for the de novo deposition of histones H3 and H4 at the DNA replication fork.


The actual alignment was detected with superfamily member pfam15539:

Pssm-ID: 434777  Cd Length: 288  Bit Score: 46.91  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    947 QDQTPEQPVPLQLDDRLMQQLVRLTHGNRNSKTFLINEYLEYLK----------------TQATAEANQTTLPSKAVLRE 1010
Cdd:pfam15539   55 EEQTPKASKREKRDQQILAQLLPLLHGNVNGSKVIIREFQEHCRrgllskgtgsppspstSRPHTPTEDAAIPSKARLKR 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   1011 KFDELASWKtvelstpeaaaasansakkgRKPKKRLCWVVASDMLEKFQLPDLQLQNQWNYtltpkVSDGPDAAQQEqsp 1090
Cdd:pfam15539  135 IISENSVYE--------------------KRPDFRMCWYVHPQVLQSFDQEHLPVPCQWSY-----VTMVPSAPRED--- 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 18858189   1091 pADAVPAASPASNqttnsaptTPIS------GQTQAGQGVKKR 1127
Cdd:pfam15539  187 -SGSVPATGPSQG--------TPISlkrksaGSMCITQFMKKR 220
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
131-603 4.85e-22

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 103.68  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   131 EDVIELDEDEADKEIEDQDQLVEAKSSKEVKLKPKKSEGKKGSPapiQIKLPLVNKRSKRRKSLKKSEEplETSTADVAK 210
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKKADAAKKKAEE--AKKAAEAAK 1349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   211 GDSESSDDIEIIAEELNPQKRQKVQTPREKSPE--NSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKK--EEPKTAEQ 286
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEE 1429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   287 NKKNDQATIDLFMGKKMETNKKDKPEVKTTAKDNKKdplIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDS 366
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   367 TTKSK---------KEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMIL 437
Cdd:PTZ00121 1507 EAKKKadeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   438 STSEANSSSSEHEMDADTDTAATDRPSAQKETRLNRKSL---PEVTGAPKGLTPKQQ---RLMEQRKKAREEKEQKLAEE 511
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAeekKKAEELKKAEEENKIKAAEE 1666
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   512 RRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKK 591
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
                         490
                  ....*....|..
gi 18858189   592 EQEREEAEQKKK 603
Cdd:PTZ00121 1747 EEAKKDEEEKKK 1758
CAF1A pfam12253
Chromatin assembly factor 1 subunit A; The CAF-1 or chromatin assembly factor-1 consists of ...
770-813 4.06e-19

Chromatin assembly factor 1 subunit A; The CAF-1 or chromatin assembly factor-1 consists of three subunits, and this is the first, or A. The A domain is uniquely required for the progression of S phase in mouse cells, independent of its ability to promote histone deposition but dependent on its ability to interact with HP1 - heterochromatin protein 1-rich heterochromatin domains next to centromeres that are crucial for chromosome segregation during mitosis. This HP1-CAF-1 interaction module functions as a built-in replication control for heterochromatin, which, like a control barrier, has an impact on S-phase progression in addition to DNA-based checkpoints.


Pssm-ID: 463507  Cd Length: 75  Bit Score: 82.55  E-value: 4.06e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 18858189    770 KYLHFADNRRPPYYGTWRKKSSSISARRPLAQDKVLFDYEVDSD 813
Cdd:pfam12253    1 KLLQFYEDVRPPYYGTWTKKSSVVGPRNPFAKDLLGLDYDYDSD 44
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
463-611 1.29e-08

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 56.64  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    463 PSAQKETRLNRKSLPEVTGAPKGLTP-------KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQ 535
Cdd:pfam13904   31 SSSQSSSLTYARKLEGLKLERQPLEAyenwlaaKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTK 110
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18858189    536 QRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:pfam13904  111 KREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
488-611 5.80e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 56.01  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    488 PKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKN 567
Cdd:TIGR02794   65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA 144
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 18858189    568 EEKRKR-------NEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:TIGR02794  145 KEEAAKqaeeeakAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 9.69e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 9.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18858189  569 EKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
CAF1-p150_C2 pfam15539
CAF1 complex subunit p150, region binding to CAF1-p60 at C-term; CAF1-p150_C2 is part of the ...
947-1127 4.40e-05

CAF1 complex subunit p150, region binding to CAF1-p60 at C-term; CAF1-p150_C2 is part of the binding region of the CAF1 complex p150 subunit to the p60 subunit. The CAF1 complex is essential in human cells for the de novo deposition of histones H3 and H4 at the DNA replication fork.


Pssm-ID: 434777  Cd Length: 288  Bit Score: 46.91  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    947 QDQTPEQPVPLQLDDRLMQQLVRLTHGNRNSKTFLINEYLEYLK----------------TQATAEANQTTLPSKAVLRE 1010
Cdd:pfam15539   55 EEQTPKASKREKRDQQILAQLLPLLHGNVNGSKVIIREFQEHCRrgllskgtgsppspstSRPHTPTEDAAIPSKARLKR 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   1011 KFDELASWKtvelstpeaaaasansakkgRKPKKRLCWVVASDMLEKFQLPDLQLQNQWNYtltpkVSDGPDAAQQEqsp 1090
Cdd:pfam15539  135 IISENSVYE--------------------KRPDFRMCWYVHPQVLQSFDQEHLPVPCQWSY-----VTMVPSAPRED--- 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 18858189   1091 pADAVPAASPASNqttnsaptTPIS------GQTQAGQGVKKR 1127
Cdd:pfam15539  187 -SGSVPATGPSQG--------TPISlkrksaGSMCITQFMKKR 220
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
251-606 7.54e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 46.93  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   251 HTEEVMQKN-----GKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLFMGKKMETNK----------KDKPEVKT 315
Cdd:NF033838   36 HAEEVRGGNnptvtSSGNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKteylyelnvlKEKSEAEL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   316 TAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKK----EKADSPANNQKEQQIGVKK 391
Cdd:NF033838  116 TSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKtlelEIAESDVEVKKAELELVKE 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   392 KTSEPEDaSNSHKSVTAKKDSKKDEAST--QVKSDNESPEAAEISMILSTSEANSSSSEHEMDADTDTAATDRPSAQKET 469
Cdd:NF033838  196 EAKEPRD-EEKIKQAKAKVESKKAEATRleKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPA 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   470 RLNRKSLPEVTGAPK--GLTPKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHRE---------QQKKQERDEKEQQRK 538
Cdd:NF033838  275 TPDKKENDAKSSDSSvgEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyptntyktlELEIAESDVKVKEAE 354
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18858189   539 LERdQKEQQRKMEKEEKERKRQAEVDSKNEE-------KRKRNEAKEEVQRKKDEERRKKEqerEEAEQKKKRAA 606
Cdd:NF033838  355 LEL-VKEEAKEPRNEEKIKQAKAKVESKKAEatrlekiKTDRKKAEEEAKRKAAEEDKVKE---KPAEQPQPAPA 425
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
495-616 2.14e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.31  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   495 EQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDE--KEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRK 572
Cdd:NF033838  128 EQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNypTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIK 207
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18858189   573 rnEAKEEVQRKKDEERRKKE--QEREEAEQKKKRAAESFSKFFVPK 616
Cdd:NF033838  208 --QAKAKVESKKAEATRLEKikTDREKAEEEAKRRADAKLKEAVEK 251
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
491-599 3.06e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAREEKEQKLAEERRLKQQdkehREQQKKQERDEKEQQRKLERDQKEQQrkmekeekeRKRQAEVDSKNEEK 570
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAEQERKLL----EEQQRELEQKLEDQERSYEEHLRQLK---------EKMEEERENLLKEQ 257
                         90       100
                 ....*....|....*....|....*....
gi 18858189  571 RKRNEAKEEVQRKKDEERRKKEQEREEAE 599
Cdd:cd16269  258 ERALESKLKEQEALLEEGFKEQAELLQEE 286
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
131-603 4.85e-22

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 103.68  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   131 EDVIELDEDEADKEIEDQDQLVEAKSSKEVKLKPKKSEGKKGSPapiQIKLPLVNKRSKRRKSLKKSEEplETSTADVAK 210
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKKADAAKKKAEE--AKKAAEAAK 1349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   211 GDSESSDDIEIIAEELNPQKRQKVQTPREKSPE--NSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKK--EEPKTAEQ 286
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEE 1429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   287 NKKNDQATIDLFMGKKMETNKKDKPEVKTTAKDNKKdplIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDS 366
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   367 TTKSK---------KEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMIL 437
Cdd:PTZ00121 1507 EAKKKadeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   438 STSEANSSSSEHEMDADTDTAATDRPSAQKETRLNRKSL---PEVTGAPKGLTPKQQ---RLMEQRKKAREEKEQKLAEE 511
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAeekKKAEELKKAEEENKIKAAEE 1666
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   512 RRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKK 591
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
                         490
                  ....*....|..
gi 18858189   592 EQEREEAEQKKK 603
Cdd:PTZ00121 1747 EEAKKDEEEKKK 1758
CAF1A pfam12253
Chromatin assembly factor 1 subunit A; The CAF-1 or chromatin assembly factor-1 consists of ...
770-813 4.06e-19

Chromatin assembly factor 1 subunit A; The CAF-1 or chromatin assembly factor-1 consists of three subunits, and this is the first, or A. The A domain is uniquely required for the progression of S phase in mouse cells, independent of its ability to promote histone deposition but dependent on its ability to interact with HP1 - heterochromatin protein 1-rich heterochromatin domains next to centromeres that are crucial for chromosome segregation during mitosis. This HP1-CAF-1 interaction module functions as a built-in replication control for heterochromatin, which, like a control barrier, has an impact on S-phase progression in addition to DNA-based checkpoints.


Pssm-ID: 463507  Cd Length: 75  Bit Score: 82.55  E-value: 4.06e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 18858189    770 KYLHFADNRRPPYYGTWRKKSSSISARRPLAQDKVLFDYEVDSD 813
Cdd:pfam12253    1 KLLQFYEDVRPPYYGTWTKKSSVVGPRNPFAKDLLGLDYDYDSD 44
PTZ00121 PTZ00121
MAEBL; Provisional
153-605 4.85e-16

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 84.04  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   153 EAKSSKEVKLKPKKSEGKKGSPAPIQIKLPLVNKRSKRR-KSLKKSEEpleTSTADVAKGDSESSDDIEIIAEELNPQKR 231
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKaDELKKAEE---KKKADEAKKAEEKKKADEAKKKAEEAKKA 1317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   232 QKVQTPREKSPENSSTSGKHTEEVMQKN----GKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQAtidlfmgKKMETNK 307
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAeaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-------KKKAEEK 1390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   308 KDKPEVKTTAKDNKKDpliAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKADSPANNQKEQQI 387
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKK---ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   388 GVKKKTSEPEDASNSHKSVTAKKdsKKDEASTQVKSDNESPEAAEISMILSTSEANSSSSEHEMDADTDTAATDRPSAQK 467
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKK--KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   468 ETRLNRKSLPEVTGAPKGLTPKQQRLMEQRKKA--REEKEQKLAEERRLKQQDKEHREQQK-KQERDEKEQQrklERDQK 544
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMalRKAEEAKKAEEARIEEVMKLYEEEKKmKAEEAKKAEE---AKIKA 1622
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18858189   545 EQQRKMEKEEKE----RKRQAEVDSKNEEKRKRNEA----KEEVQRKKDEERRKKEQEREEAEQKKKRA 605
Cdd:PTZ00121 1623 EELKKAEEEKKKveqlKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
PTZ00121 PTZ00121
MAEBL; Provisional
185-611 1.57e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 75.95  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   185 NKRSKRRKSLKKSEEPLETSTADVAKGDSESSDDIEII-AEELNPQKRQKVQTPREKSPENSSTSGKHTEEVMQKNGKDS 263
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGkAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA 1151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   264 KKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLFMGKKMETNKKD---KPEVKTTAKDNKKdpliAEDSKPKEVPKKET 340
Cdd:PTZ00121 1152 KRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarKAEAARKAEEERK----AEEARKAEDAKKAE 1227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   341 SKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQ 420
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   421 VKSDNESPEAAEISMILSTSEANSSSSEHEMDADTDTAATDRPSAQKETRLNRKSLPEVTGAPKGLTPKQQRLMEQRKKA 500
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   501 rEEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEV 580
Cdd:PTZ00121 1388 -EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
                         410       420       430
                  ....*....|....*....|....*....|..
gi 18858189   581 Q-RKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:PTZ00121 1467 EeAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
PTZ00121 PTZ00121
MAEBL; Provisional
139-595 8.41e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 73.25  E-value: 8.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   139 DEADKEIEDQDQLVEAKSSKEVKLKPKKSEGKKGSPAPiqiKLPLVNKRSKRRKSLKKSEEPLETSTADV-AKGDSESSD 217
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKKKADAAKKKAEEKKKADEAKKkAEEDKKKAD 1408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   218 DIEIIAEELNP--QKRQKVQTPREKSPENSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKK--EEPKTAEQNKKNDQA 293
Cdd:PTZ00121 1409 ELKKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEA 1488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   294 TIDLFMGKKMETNKKDKPEVKTTAKDNKK--DPLIAEDSKPKEVPKK--ETSKTGGKGKKEGAKPAEKSKKEEKEDSTTK 369
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKadEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   370 SKKEKADSPANNQKEQQI--GVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMILSTSEANSSSS 447
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   448 EHEMDADTDTAATDRPSAQKETRLNRKSLPEVTGAPKGLTPKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKK 527
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   528 QERDEKEQQRKLERDQKEQQRKMEKEEKERKRQ--AEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQER 595
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
PTZ00121 PTZ00121
MAEBL; Provisional
193-607 3.65e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 71.33  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   193 SLKKSEEPLETSTADVAKGDSESSDDIEIIAEELNPQKRQKVQTPREKSPensstSGKHTEEVMQKNGKDSKKQEESMKA 272
Cdd:PTZ00121 1025 NIEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKP-----SYKDFDFDAKEDNRADEATEEAFGK 1099
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   273 VKESKKEEPKTAEQNKKNDQATIDLFMGKKMETNKKDKPEVKTTAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGA 352
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   353 KPAEKSKKEEKEDSTTKSKKEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAE 432
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   433 ISMILSTSEANSSSSEHEMDADTDTAATDRPSAQKETRLNRKSLPEvtgAPKGLTPKQQRLMEQRKKAREEKeqKLAEER 512
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD---EAKKKAEEAKKADEAKKKAEEAK--KKADAA 1334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   513 RLKQQDKEHREQQKKQErdEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKE--EVQRKKDEERRK 590
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAE--AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKK 1412
                         410
                  ....*....|....*..
gi 18858189   591 KEQEREEAEQKKKRAAE 607
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEE 1429
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
463-611 1.29e-08

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 56.64  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    463 PSAQKETRLNRKSLPEVTGAPKGLTP-------KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQ 535
Cdd:pfam13904   31 SSSQSSSLTYARKLEGLKLERQPLEAyenwlaaKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTK 110
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18858189    536 QRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:pfam13904  111 KREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
488-611 5.80e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 56.01  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    488 PKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKN 567
Cdd:TIGR02794   65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA 144
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 18858189    568 EEKRKR-------NEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:TIGR02794  145 KEEAAKqaeeeakAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
489-683 7.31e-08

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: 56.67  E-value: 7.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:pfam17380  390 KNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    569 EKRKRNEA---KEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSKFFVPKQPKcgsgSNNTSYLEHEQSSCDSSKASSQ 645
Cdd:pfam17380  470 EERKRKKLeleKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEME----ERQKAIYEEERRREAEEERRKQ 545
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 18858189    646 TLAFRPFQIKDDMLLApivrnslgQEQRSQLDGLFRHR 683
Cdd:pfam17380  546 QEMEERRRIQEQMRKA--------TEERSRLEAMERER 575
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 9.69e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 9.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18858189  569 EKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
490-611 1.18e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.58  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   490 QQRLMEQRKKAREEKEQKLAEERRLKQQdkehrEQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEE 569
Cdd:PRK09510   79 EQRKKKEQQQAEELQQKQAAEQERLKQL-----EKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA 153
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 18858189   570 KRKRNEAK---EEVQRKKDEERRKKeqerEEAEQKKKRAAESFSK 611
Cdd:PRK09510  154 KRAAAAAKkaaAEAKKKAEAEAAKK----AAAEAKKKAEAEAAAK 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
491-607 2.12e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEK 570
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18858189  571 RKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 3.12e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKE------QQRKLERDQKEQQRKMEKEEKERKRQAE 562
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeaeeelEEAEAELAEAEEALLEAEAELAEAEEEL 381
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18858189  563 VDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 4.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLME-QRKKAREEKEQKLAEERRlkqQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKN 567
Cdd:COG1196  286 AQAEEYElLAELARLEQDIARLEERR---RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18858189  568 EEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
465-607 4.62e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  465 AQKETRLNRKSLPEVTgapKGLTPKQQRLME-QRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQ 543
Cdd:COG1196  286 AQAEEYELLAELARLE---QDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18858189  544 KEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKK--EQEREEAEQKKKRAAE 607
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEalLERLERLEEELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 5.71e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18858189  569 EKRKR--NEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  397 ELAAQleELEEAEEALLERLERLEEELEELEEALAELEEEE 437
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
493-607 9.06e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 49.65  E-value: 9.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    493 LMEQRKKAREEKEQKlaEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEkeekerkrqaevdSKNEEKRK 572
Cdd:pfam05672   16 LAEKRRQAREQRERE--EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------------EEEERQRK 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 18858189    573 RNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam05672   81 AEEEAEEREQREQEEQERLQKQKEEAEAKAREEAE 115
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
492-611 9.26e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.50  E-value: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   492 RLMEQRKKAR--EEKEQKLAEERRLKQQDKEHREQQKKQERdekEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEE 569
Cdd:PRK09510   66 RQQQQQKSAKraEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 18858189   570 KRKRNEAKEEVQRKKDEERRKKE--QEREEAEQKKKRAAESFSK 611
Cdd:PRK09510  143 AAAKAKAEAEAKRAAAAAKKAAAeaKKKAEAEAAKKAAAEAKKK 186
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
491-611 1.20e-06

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: 52.07  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQrkmekeekerkrQAEVDSKNEEK 570
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ------------KLLARLEKELA 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18858189  571 RKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:COG4942  210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
PTZ00121 PTZ00121
MAEBL; Provisional
139-604 3.97e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   139 DEADKEIEDQDQLVEAKSSKEVKLKPKKSEgKKGSPAPIQIKLPLVNKRSKRRKSLKKSEEplETSTADVAKGDSESSDD 218
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAE--EAKKADEAKKKAEEAKK 1497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   219 IeiiAEELNPQKRQKVQTPREKSPENSSTSGKHTEEVMQKNGKDSKKQEESMKA-----VKESKKEEPKTAEQNKKNDQA 293
Cdd:PTZ00121 1498 K---ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdelkkAEELKKAEEKKKAEEAKKAEE 1574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   294 TIDLFMGKKMETNKKDKPEVKTTAKDNKKDpliaEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKE 373
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEE----KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   374 KADSPANNQKEQQIGVKKKtsEPEDASNSHKSVTAKKDSKKdeASTQVKSDNESPEAAEismILSTSEANSSSSEHEMDA 453
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAE---ELKKKEAEEKKKAEELKK 1723
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   454 DTDTAATDRPSAQKETRLNRKSLPEVTGAPKGLTPKQQRLMEQRKKAREEKEQKLAE-ERRLKQQDKEHREQQKKQERDE 532
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDI 1803
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18858189   533 KEQQRKLERDQKEQQRKMEKEEKERKRQAE--VDSKNEEkrkRNEAKEEVQRKKDEERRKKEQEREEAEQKKKR 604
Cdd:PTZ00121 1804 FDNFANIIEGGKEGNLVINDSKEMEDSAIKevADSKNMQ---LEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
489-605 4.19e-06

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.64  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEqklaeerRLKQQDKEHREQQkkQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKnE 568
Cdd:COG2268  229 EQEREIETARIAEAEAE-------LAKKKAEERREAE--TARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEK-E 298
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18858189  569 EKRKRNEAKEEVqRKKDEERRKKEQEREEAEQKKKRA 605
Cdd:COG2268  299 AEREEAELEADV-RKPAEAEKQAAEAEAEAEAEAIRA 334
PTZ00121 PTZ00121
MAEBL; Provisional
365-617 4.59e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   365 DSTTKSKKEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMILSTSEANS 444
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   445 SSSEHEMDADTDTAATDRPSAQKETRLNRKSlPEVTGAPKGLTPKQQRLMEQRKKARE----EKEQKLAEERRLKQQDKE 520
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKA-EELRKAEDARKAEAARKAEEERKAEEarkaEDAKKAEAVKKAEEAKKD 1238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   521 HREQQKKQERDEKEQQRKLERDQ-------------KEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKE--EVQRKKD 585
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARmahfarrqaaikaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaEEAKKAD 1318
                         250       260       270
                  ....*....|....*....|....*....|..
gi 18858189   586 EERRKKEQEREEAEQKKKRAAESFSKFFVPKQ 617
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 4.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQK--KQERDEKEQQRK--LERDQKEQQRKMEKEEKERKRQAEVD 564
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRelEERLEELEEELAelEEELEELEEELEELEEELEEAEEELE 354
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18858189  565 SKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
462-606 5.66e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 50.34  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    462 RPSAQKETRLNRKSLPEVTGAPKGLTPKQQRLMEQ---RKKAREEKEQKLAEERRlKQQDKEHREQQKKQERDEKEQQRK 538
Cdd:pfam15709  354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirlRKQRLEEERQRQEEEER-KQRLQLQAAQERARQQQEEFRRKL 432
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18858189    539 LERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKR-----NEAKEEVQRKKDEERRKKEQEREEAEQKKKRAA 606
Cdd:pfam15709  433 QELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmemaEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA 505
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
146-418 9.64e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 50.04  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   146 EDQDQLVEAKSSKEVKLKPKKSEGKKGSPAPIQIKLPlvnkrsKRRKSLKKSEEPLETSTADVAKGDSESSDDIEIIAEE 225
Cdd:PTZ00108 1132 EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK------LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDE 1205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   226 lnpqKRQKVQTPREKSPENSSTSGKHTEEvmqkngKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLfmgkkmET 305
Cdd:PTZ00108 1206 ----KRKLDDKPDNKKSNSSGSDQEDDEE------QKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSK------EG 1269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   306 NKKDKPEVKTTAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTT---KSKKEKADSPAN-- 380
Cdd:PTZ00108 1270 KPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTArkkKSKTRVKQASASqs 1349
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 18858189   381 NQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEAS 418
Cdd:PTZ00108 1350 SRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDDEDD 1387
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
491-607 1.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAreEKEQKLAEERRLKQ------QDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVD 564
Cdd:COG1196  203 EPLERQAEKA--ERYRELKEELKELEaellllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18858189  565 SKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
490-607 1.68e-05

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.19  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    490 QQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEE 569
Cdd:pfam05672   26 QREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEE 105
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 18858189    570 KRKRneAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam05672  106 AEAK--AREEAERQRQEREKIMQQEEQERLERKKRIEE 141
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 2.44e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQK-EQQRKMEKEEKERKRQAEVDSKN 567
Cdd:COG1196  250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELE 329
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18858189  568 EEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
PTZ00121 PTZ00121
MAEBL; Provisional
104-415 3.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   104 RRSTSKENLDLASSIATKKVKTTDSVVEDVIELDEDEADKEIEDQDQLVEAKSSKEVKLKP-----------KKSEGKKG 172
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqlkkkeaeekKKAEELKK 1654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   173 SPAPIQIKLPLVNKRS---KRRKSLKKSEEPLETSTADVAKGDSESSDDIEIIAEELNPQKRQKVQTPR-EKSPENSSTS 248
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaEEENKIKAEE 1734
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   249 GKHTEEVMQKNGKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLFMGKKmetNKKDKPEVKTTAKD--------- 319
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE---DEKRRMEVDKKIKDifdnfanii 1811
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   320 --NKKDPLIAEDSKPKEvpkketsktggkgkkegakpaekskkeekeDSTTKSKKEKADSPANNQKEQQIGVKKKTSEPE 397
Cdd:PTZ00121 1812 egGKEGNLVINDSKEME------------------------------DSAIKEVADSKNMQLEEADAFEKHKFNKNNENG 1861
                         330
                  ....*....|....*...
gi 18858189   398 DASNSHKSVTAKKDSKKD 415
Cdd:PTZ00121 1862 EDGNKEADFNKEKDLKED 1879
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
490-607 3.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  490 QQRLMEQRKKAREEKEQKLAEERRlKQQDKEHREQQKKQERDEKEQQRkLERDQKEQQRKMEKEEKERKRQAEVDSKNEE 569
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18858189  570 KRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
507-594 3.12e-05

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 46.19  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    507 KLAEERRLKQQDKEHREQQKKQERDEKEQQRKLErDQKEQqrkmekeekerkrqaEVDSKNEEKRKRNEAKEEVQRKKDE 586
Cdd:pfam09756    2 KLGAKKRAKLELKEAKRQQREAEEEEREEREKLE-EKREE---------------EYKEREEREEEAEKEKEEEERKQEE 65

                   ....*...
gi 18858189    587 ERRKKEQE 594
Cdd:pfam09756   66 EQERKEQE 73
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-611 3.67e-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: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERD-QKEQQRKMEKEEKERKRQAEVDSKN 567
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYElLAELARLEQDIARLEERRRELEERL 318
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18858189  568 EEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
CAF1-p150_C2 pfam15539
CAF1 complex subunit p150, region binding to CAF1-p60 at C-term; CAF1-p150_C2 is part of the ...
947-1127 4.40e-05

CAF1 complex subunit p150, region binding to CAF1-p60 at C-term; CAF1-p150_C2 is part of the binding region of the CAF1 complex p150 subunit to the p60 subunit. The CAF1 complex is essential in human cells for the de novo deposition of histones H3 and H4 at the DNA replication fork.


Pssm-ID: 434777  Cd Length: 288  Bit Score: 46.91  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    947 QDQTPEQPVPLQLDDRLMQQLVRLTHGNRNSKTFLINEYLEYLK----------------TQATAEANQTTLPSKAVLRE 1010
Cdd:pfam15539   55 EEQTPKASKREKRDQQILAQLLPLLHGNVNGSKVIIREFQEHCRrgllskgtgsppspstSRPHTPTEDAAIPSKARLKR 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   1011 KFDELASWKtvelstpeaaaasansakkgRKPKKRLCWVVASDMLEKFQLPDLQLQNQWNYtltpkVSDGPDAAQQEqsp 1090
Cdd:pfam15539  135 IISENSVYE--------------------KRPDFRMCWYVHPQVLQSFDQEHLPVPCQWSY-----VTMVPSAPRED--- 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 18858189   1091 pADAVPAASPASNqttnsaptTPIS------GQTQAGQGVKKR 1127
Cdd:pfam15539  187 -SGSVPATGPSQG--------TPISlkrksaGSMCITQFMKKR 220
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
489-607 4.57e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.11  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQrKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:PRK09510  102 RLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 18858189   569 EKRKRNEAKEEVQRKKDEERRKKEQEREE---AEQKKKRAAE 607
Cdd:PRK09510  181 AEAKKKAEAEAAAKAAAEAKKKAEAEAKKkaaAEAKKKAAAE 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
492-607 4.73e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  492 RLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRK-LERDQKEQQRKMEKEEKERKRQAEVDSKNEEK 570
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeLEEAQAEEYELLAELARLEQDIARLEERRREL 314
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18858189  571 RKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
488-607 4.83e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.15  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    488 PKQQRLMEQRKKAREEKEQKLAEERRlKQQDKEHREQQKKQERDEKEQQRKLE----RDQKEQQRKMEKEEKERKRQAEV 563
Cdd:TIGR02794   86 AEQARQKELEQRAAAEKAAKQAEQAA-KQAEEKQKQAEEAKAKQAAEAKAKAEaeaeRKAKEEAAKQAEEEAKAKAAAEA 164
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 18858189    564 DSKNEEKRKRNE----AKEEVQRKKDEERRKKEQE----REEAEQKKKRAAE 607
Cdd:TIGR02794  165 KKKAEEAKKKAEaeakAKAEAEAKAKAEEAKAKAEaakaKAAAEAAAKAEAE 216
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
478-606 5.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  478 EVTGAPKGLTPKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHRE--QQKKQERDEKEQQRKLERDQKEQQRKMEKEEK 555
Cdd:COG1196  648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELelEEALLAEEEEERELAEAEEERLEEELEEEALE 727
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18858189  556 ERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAA 606
Cdd:COG1196  728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
251-606 7.54e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 46.93  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   251 HTEEVMQKN-----GKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLFMGKKMETNK----------KDKPEVKT 315
Cdd:NF033838   36 HAEEVRGGNnptvtSSGNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKteylyelnvlKEKSEAEL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   316 TAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKK----EKADSPANNQKEQQIGVKK 391
Cdd:NF033838  116 TSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKtlelEIAESDVEVKKAELELVKE 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   392 KTSEPEDaSNSHKSVTAKKDSKKDEAST--QVKSDNESPEAAEISMILSTSEANSSSSEHEMDADTDTAATDRPSAQKET 469
Cdd:NF033838  196 EAKEPRD-EEKIKQAKAKVESKKAEATRleKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPA 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   470 RLNRKSLPEVTGAPK--GLTPKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHRE---------QQKKQERDEKEQQRK 538
Cdd:NF033838  275 TPDKKENDAKSSDSSvgEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyptntyktlELEIAESDVKVKEAE 354
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18858189   539 LERdQKEQQRKMEKEEKERKRQAEVDSKNEE-------KRKRNEAKEEVQRKKDEERRKKEqerEEAEQKKKRAA 606
Cdd:NF033838  355 LEL-VKEEAKEPRNEEKIKQAKAKVESKKAEatrlekiKTDRKKAEEEAKRKAAEEDKVKE---KPAEQPQPAPA 425
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
252-604 1.01e-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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.89  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    252 TEEVMQKNGKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLFMGKKMETNKkdkpeVKTTAKDNKKDPLIAED-- 329
Cdd:pfam02463  678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-----INEELKLLKQKIDEEEEee 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    330 --SKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVT 407
Cdd:pfam02463  753 ekSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    408 AKKDSKKDEASTQVKSDNESPEAAEISMILSTSEANSSSSEHEMDADTDTAATDRpSAQKETRLNRKSLPEVTgapkglt 487
Cdd:pfam02463  833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE-LESKEEKEKEEKKELEE------- 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    488 pKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKN 567
Cdd:pfam02463  905 -ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 18858189    568 EEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKR 604
Cdd:pfam02463  984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
500-611 1.26e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    500 AREEKEQKLAEERRLKQQDKEHREQQKKQERdEKEQQRKLERDQKEQQRKME------KEEKERKRQAEVDSKNEEKRKR 573
Cdd:TIGR02794   56 QQQKKPAAKKEQERQKKLEQQAEEAEKQRAA-EQARQKELEQRAAAEKAAKQaeqaakQAEEKQKQAEEAKAKQAAEAKA 134
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 18858189    574 NEAKEEVQRKKDEERRKKEQER--EEAEQKKKRAAESFSK 611
Cdd:TIGR02794  135 KAEAEAERKAKEEAAKQAEEEAkaKAAAEAKKKAEEAKKK 174
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
489-604 1.53e-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: 45.29  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQ-----ERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEV 563
Cdd:pfam13868   63 KEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEW 142
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 18858189    564 DSKNEEKRKRNEAK-EEVQRKKDEERRKKEQEREEAEQKKKR 604
Cdd:pfam13868  143 KELEKEEEREEDERiLEYLKEKAEREEEREAEREEIEEEKER 184
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
489-607 1.59e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQR-KLERDQKEQQRKMEKEEKERKRQAEVDSK- 566
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRlELEELELELEEAQAEEYELLAELARLEQDi 304
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18858189  567 --NEEKRKRNEAKEEvqrKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG1196  305 arLEERRRELEERLE---ELEEELAELEEELEELEEELEELEE 344
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
495-596 2.16e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.03  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    495 EQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERkrQAEVDSKNEEKRKRN 574
Cdd:pfam15558   36 ELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWRE--QAEDQENQRQEKLER 113
                           90       100
                   ....*....|....*....|..
gi 18858189    575 EAKEEVQRKKDEERRKKEQERE 596
Cdd:pfam15558  114 ARQEAEQRKQCQEQRLKEKEEE 135
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
496-618 2.22e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 44.98  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    496 QRKKAREEKEQKLAEERRLKQqdkEHREQQKKQERDEK-EQQRKLERDQKEQQRKMEKEEKERKRQAEVDS-KNEEKRKR 573
Cdd:pfam07767  206 EAEKKRLKEEEKLERVLEKIA---ESAATAEAREEKRKtKAQRNKEKRRKEEEREAKEEKALKKKLAQLERlKEIAKEIA 282
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 18858189    574 NEAKEEVQRKKDEERRKKEQEREEAEQKKKRaaesFSKFFVPKQP 618
Cdd:pfam07767  283 EKEKEREEKAEARKREKRKKKKEEKKLRPRK----LGKHKVPEPD 323
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
490-607 2.48e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 2.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    490 QQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEE 569
Cdd:pfam13868   42 ERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK 121
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 18858189    570 KRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam13868  122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
489-607 4.57e-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: 43.75  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQ-----KKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEV 563
Cdd:pfam13868  167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERdelraKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE 246
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 18858189    564 DSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam13868  247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
PRK08581 PRK08581
amidase domain-containing protein;
241-437 4.59e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.39  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   241 SPENSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKKEEPK------TAEQNKKNDQATIDLFMGKKMETNKKDKPEVK 314
Cdd:PRK08581   31 QKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDnndkkfSTIDSSTSDSNNIIDFIYKNLPQTNINQLLTK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   315 TTAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKADSP----ANNQKEQQIGVK 390
Cdd:PRK08581  111 NKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNQkapsSNNTKPSTSNKQ 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 18858189   391 KKTSEPEDASNSHKSVTAKKDSKKDEAStqvkSDNESPEAAEISMIL 437
Cdd:PRK08581  191 PNSPKPTQPNQSNSQPASDDTANQKSSS----KDNQSMSDSALDSIL 233
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
525-604 5.23e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 42.33  E-value: 5.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    525 QKKQERDEKEQQRKLERDQKEQQRkmekeekerkrqaevdsknEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKR 604
Cdd:pfam09756    5 AKKRAKLELKEAKRQQREAEEEER-------------------EEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEE 65
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
482-598 6.12e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.84  E-value: 6.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    482 APKGLTPKQQRLMEQRKKA----------REEKEQKLAEERRL--------KQQDKEHREQQKKQ-ERDEKEQQRKLERD 542
Cdd:pfam05262  218 LKEELDKKQIDADKAQQKAdfaqdnadkqRDEVRQKQQEAKNLpkpadtssPKEDKQVAENQKREiEKAQIEIKKNDEEA 297
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 18858189    543 QK--EQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEA 598
Cdd:pfam05262  298 LKakDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
489-607 7.26e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLaEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQA---EVDS 565
Cdd:pfam17380  366 RQEEIAMEISRMRELERLQM-ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVrrlEEER 444
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 18858189    566 KNEEKRKRNEAKE-----EVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam17380  445 AREMERVRLEEQErqqqvERLRQQEEERKRKKLELEKEKRDRKRAEE 491
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
491-593 9.00e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 9.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   491 QRLMEQRKKAreekEQKLAE-ERRLKQQDKEHRE-QQKKQERDEKEQQRKLERDQKEQQ-----------RKMEKEEKER 557
Cdd:PRK00409  523 ASLEELEREL----EQKAEEaEALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQQaikeakkeadeIIKELRQLQK 598
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18858189   558 KRQAEVDSKN-EEKRKR-NEAKEEVQRKKDEERRKKEQ 593
Cdd:PRK00409  599 GGYASVKAHElIEARKRlNKANEKKEKKKKKQKEKQEE 636
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
515-607 1.03e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.91  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    515 KQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQE 594
Cdd:TIGR02794   49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128
                           90
                   ....*....|...
gi 18858189    595 REEAEQKKKRAAE 607
Cdd:TIGR02794  129 AAEAKAKAEAEAE 141
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
498-547 1.11e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.55  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 18858189    498 KKAREEKEQKLAEERRLKQQD--KEHREQQKKQERDEK------EQQRKLERDQKEQQ 547
Cdd:pfam07946  263 KKTREEEIEKIKKAAEEERAEeaQEKKEEAKKKEREEKlaklspEEQRKYEEKERKKE 320
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
489-612 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAE-ERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEK-EEKERKRQAEVDSK 566
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDaEERLAKLEAEIDKL 334
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 18858189    567 NEEKRKRNEAKEEVQRKKD---EERRKKEQERE----EAEQKKKRAAESFSKF 612
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDkltEEYAELKEELEdlraELEEVDKEFAETRDEL 387
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
504-595 1.24e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.58  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    504 KEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQrkmekeekerkrqaevdsKNEEKRKRNEAKEEVQRK 583
Cdd:pfam15927    1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEE------------------LEELKHLLEERKEALEKL 62
                           90
                   ....*....|..
gi 18858189    584 KDEERRKKEQER 595
Cdd:pfam15927   63 RAEAREEAEWER 74
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
223-433 1.61e-03

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 42.29  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   223 AEELNPQKRQKVQTPREKSPENSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQAtidlfmgKK 302
Cdd:PRK05901    5 STKAELAAEEEAKKKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIP-------KK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   303 METNKKDKPEVKTTAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKAD------ 376
Cdd:PRK05901   78 KTKTAAKAAAAKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDddeddd 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18858189   377 -SPANNQKEQQIGVKKKTSEPEDASnshKSVTAKKDSKKDEASTQVKSDNESPEAAEI 433
Cdd:PRK05901  158 eDDDDDDVDDEDEEKKEAKELEKLS---DDDDFVWDEDDSEALRQARKDAKLTATADP 212
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
490-607 1.80e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    490 QQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDsKNEE 569
Cdd:pfam13868  139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE-EQER 217
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 18858189    570 KRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEE 255
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
495-616 2.14e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.31  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   495 EQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDE--KEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRK 572
Cdd:NF033838  128 EQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNypTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIK 207
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18858189   573 rnEAKEEVQRKKDEERRKKE--QEREEAEQKKKRAAESFSKFFVPK 616
Cdd:NF033838  208 --QAKAKVESKKAEATRLEKikTDREKAEEEAKRRADAKLKEAVEK 251
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
489-611 2.18e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.78  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQqrkmekeekerkrQAEVDSKNE 568
Cdd:COG2268  249 KKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAEL-------------EADVRKPAE 315
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18858189  569 EKRKRNEAKEEVQRKKDEERRKKEQereEAEQKKKRAAESFSK 611
Cdd:COG2268  316 AEKQAAEAEAEAEAEAIRAKGLAEA---EGKRALAEAWNKLGD 355
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
495-607 2.22e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    495 EQRKKAREEKEQKLAEERRLKQ---QDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKR 571
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQareEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 18858189    572 KRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam13868  298 QIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
rne PRK10811
ribonuclease E; Reviewed
498-608 2.24e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.33  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   498 KKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQR--KLERDQKEQ---------QRKMEKEEKERKRQAEVDSK 566
Cdd:PRK10811  585 ETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRdnRTRREGRENreenrrnrrQAQQQTAETRESQQAEVTEK 664
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18858189   567 -NEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAES 608
Cdd:PRK10811  665 aRTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQET 707
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
489-606 2.31e-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: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERR-LKQQDKEHREQQKKQERDEKEQQRKLER--DQKEQQRKMEKEEKERKRQAEVDS 565
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAqLELQIASLNNEIERLEARLERLEDRRERlqQEIEELLKKLEEAELKELQAELEE 444
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 18858189    566 KN---EEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAA 606
Cdd:TIGR02168  445 LEeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
489-607 2.31e-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: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEhrEQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:pfam13868  117 EAEEKLEKQRQLREEIDEFNEEQAEWKELEKE--EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE 194
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 18858189    569 EKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam13868  195 KAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQ 233
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
390-603 2.35e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    390 KKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAA--------EISMILSTSEANSSSSEHEMDADTDTAATD 461
Cdd:pfam02463  650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKeeilrrqlEIKKKEQREKEELKKLKLEAEELLADRVQE 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    462 RPSAQKETRLNRKSLPEVTGAPKGLTPKQQRLMEQRKKAREEKEQKLAEER-----RLKQQDKEH--REQQKKQERDEKE 534
Cdd:pfam02463  730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERektekLKVEEEKEEklKAQEEELRALEEE 809
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18858189    535 QQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKK 603
Cdd:pfam02463  810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
489-606 2.99e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.86  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   489 KQQRLmEQRKKAREEKEQKLAEERRLKQQD-----KEHREQQKKQERDEKEQQRKLERDQKEQ----QRKMEKEEKERKR 559
Cdd:PRK05035  458 RQARL-EREKAAREARHKKAAEARAAKDKDavaaaLARVKAKKAAATQPIVIKAGARPDNSAViaarEARKAQARARQAE 536
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18858189   560 QAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAA 606
Cdd:PRK05035  537 KQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA 583
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
491-599 3.06e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAREEKEQKLAEERRLKQQdkehREQQKKQERDEKEQQRKLERDQKEQQrkmekeekeRKRQAEVDSKNEEK 570
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAEQERKLL----EEQQRELEQKLEDQERSYEEHLRQLK---------EKMEEERENLLKEQ 257
                         90       100
                 ....*....|....*....|....*....
gi 18858189  571 RKRNEAKEEVQRKKDEERRKKEQEREEAE 599
Cdd:cd16269  258 ERALESKLKEQEALLEEGFKEQAELLQEE 286
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
489-607 3.24e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEkEQKLAEERRLKQQDKEHREQQKKqeRDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEvdSKNE 568
Cdd:pfam20492    6 REKQELEERLKQYEE-ETKKAQEELEESEETAEELEEER--RQAEEEAERLEQKRQEAEEEKERLEESAEMEAE--EKEQ 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 18858189    569 EKRKRNEAKEEVQRKKdEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam20492   81 LEAELAEAQEEIARLE-EEVERKEEEARRLQEELEEARE 118
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
494-608 3.27e-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: 41.65  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    494 MEQrKKAREEKEQKLAE-ERRLKQQDKEHREQQK---------KQERDEKEQQRKLERDQKEQQRKMEKEEKERK----- 558
Cdd:pfam17380  296 MEQ-ERLRQEKEEKAREvERRRKLEEAEKARQAEmdrqaaiyaEQERMAMERERELERIRQEERKRELERIRQEEiamei 374
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 18858189    559 --------RQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAES 608
Cdd:pfam17380  375 srmrelerLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA 432
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
491-607 3.41e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   491 QRLMEQRKKAREEKEQKLAEERR----LKQQDKEHREQ-QKKQERDEKEQQR--KLERDQKEQQRKMEKEEKERKRQAEV 563
Cdd:PRK02224  522 EELIAERRETIEEKRERAEELREraaeLEAEAEEKREAaAEAEEEAEEAREEvaELNSKLAELKERIESLERIRTLLAAI 601
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18858189   564 DSKNEEKRKRNEAKEEVQRKKDEER--------RKKEQER-------EEAEQKKKRAAE 607
Cdd:PRK02224  602 ADAEDEIERLREKREALAELNDERRerlaekreRKRELEAefdeariEEAREDKERAEE 660
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
473-611 3.69e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  473 RKSLPEvtgAPKGLTPKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQE------RDEKEQ---QRKLERDQ 543
Cdd:COG1579   26 LKELPA---ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYealQKEIESLK 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18858189  544 KEQQRKMEK----EEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSK 611
Cdd:COG1579  103 RRISDLEDEilelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
491-608 4.51e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    491 QRLMEQRKKAREEKEQKLAEERRLK--QQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:pfam02463  200 LKLKEQAKKALEYYQLKEKLELEEEylLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 18858189    569 EKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAES 608
Cdd:pfam02463  280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
489-607 4.83e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQErdeKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNE 568
Cdd:pfam02463  279 KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE 355
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 18858189    569 EKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam02463  356 EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
491-607 4.88e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKleRDQKEQQRKMEKEEKERKRQAEVDSKNEEK 570
Cdd:COG4717  128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL--QEELEELLEQLSLATEEELQDLAEELEELQ 205
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18858189  571 RKRNEAKEEVQRKKdEERRKKEQEREEAEQKKKRAAE 607
Cdd:COG4717  206 QRLAELEEELEEAQ-EELEELEEELEQLENELEAAAL 241
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
164-547 5.13e-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: 40.88  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    164 PKKSEGKKGSPAPIQiklplvnkRSKRRKSLKKSEEPLETSTAD-VAKGDSESSDDIEIIAEELNPQKRQKVQTPREKsp 242
Cdd:pfam17380  220 PKEVQGMPHTLAPYE--------KMERRKESFNLAEDVTTMTPEyTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQ-- 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    243 ensstsgKHTEEVMQKNGKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATI-----DLFMGKKMETNKKDKPEVKTTA 317
Cdd:pfam17380  290 -------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIyaeqeRMAMERERELERIRQEERKREL 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    318 KDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKADSPaNNQKEQQIGVKKKTSEPE 397
Cdd:pfam17380  363 ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME-QIRAEQEEARQREVRRLE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    398 DASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMilstseanssssEHEMDADTDTAATDRPSAQKETRLNRKSLP 477
Cdd:pfam17380  442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL------------EKEKRDRKRAEEQRRKILEKELEERKQAMI 509
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18858189    478 EVTGAPKGLtpkqQRLMEQRKKA-REEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQ 547
Cdd:pfam17380  510 EEERKRKLL----EKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
523-616 6.10e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 38.45  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   523 EQQKKQERDEKEqqrKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKK 602
Cdd:PRK07353   45 RAEAKERLAEAE---KLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQL 121
                          90
                  ....*....|....
gi 18858189   603 KRAAESFSKFFVPK 616
Cdd:PRK07353  122 EQQVDALSRQILEK 135
PRK12704 PRK12704
phosphodiesterase; Provisional
495-610 7.38e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189   495 EQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDE-KEQQRKLErdQKEQQrkmekeekerkrqaeVDSKNEEKRKR 573
Cdd:PRK12704   46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElQKLEKRLL--QKEEN---------------LDRKLELLEKR 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18858189   574 N---EAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFS 610
Cdd:PRK12704  109 EeelEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
489-613 7.70e-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: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    489 KQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKE--QQRKLERDQKEQQRKMEKEEKERKRQAEVDSK 566
Cdd:pfam13868  191 AQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQElqQAREEQIELKERRLAEEAEREEEEFERMLRKQ 270
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 18858189    567 NEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSKFF 613
Cdd:pfam13868  271 AEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEG 317
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
491-612 8.16e-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: 8.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189  491 QRLMEQRKKAREEKE--QKLAEER-RLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKN 567
Cdd:COG4913  671 AELEAELERLDASSDdlAALEEQLeELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 18858189  568 EEKRKRNEAKEEVQRKKDEE-RRKKEQEREEAEQKKKRAAESFSKF 612
Cdd:COG4913  751 LEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAF 796
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
473-607 9.30e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 9.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858189    473 RKSLPEVTGAPKGLTPKQQRLMEQRKKAR-EEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKME 551
Cdd:pfam15709  296 RSSPTQTFVVTGNMESEEERSEEDPSKALlEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMR 375
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858189    552 KEEkerkrQAEVDSKNEEKRKRNEA-KEEVQRKKDEERRKKEQEREEAEQKKKRAAE 607
Cdd:pfam15709  376 EEL-----ELEQQRRFEEIRLRKQRlEEERQRQEEEERKQRLQLQAAQERARQQQEE 427
 
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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