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Conserved domains on  [gi|41152097|ref|NP_005079|]
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A-kinase anchor protein 17A isoform 1 [Homo sapiens]

Protein Classification

RNA-binding protein; RNA-binding protein 43( domain architecture ID 10188106)

RNA-binding protein containing an RNA recognition motif (RRM)| RNA-binding protein 43 (RBM43) is an RNA-binding protein containing an RNA recognition motif (RRM)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_AKAP17A cd12264
RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar ...
 143-265 4.25e-81

RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins; This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


:

Pssm-ID: 409708 [Multi-domain]  Cd Length: 122  Bit Score: 252.96  E-value: 4.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 143 GERPDTIHLEGLPCKWFALKESgSEKPSEDVLVKVFEKFGEIRNVDIPMLDPYREEMTGRNFHTFSFGGHLNFEAYVQYR 222
Cdd:cd12264   1 GERPDTIHLEGLPCKWFAVPRS-SDKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGGHLHFEAYVQYE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 41152097 223 EYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKHLSD 265
Cdd:cd12264  80 EYDGFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE 122
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-443 9.19e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 9.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 329 QRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQS----IRLIAELLSRAKAVKLREQEQKEEKLRLQQQE 404
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELAELEEELEELEEELEELEEELEEAE 350

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41152097 405 ERRRLQEAELRRVEEEKERALGLQRKERELRERLLSILL 443
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
 
Name Accession Description Interval E-value
RRM_AKAP17A cd12264
RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar ...
 143-265 4.25e-81

RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins; This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409708 [Multi-domain]  Cd Length: 122  Bit Score: 252.96  E-value: 4.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 143 GERPDTIHLEGLPCKWFALKESgSEKPSEDVLVKVFEKFGEIRNVDIPMLDPYREEMTGRNFHTFSFGGHLNFEAYVQYR 222
Cdd:cd12264   1 GERPDTIHLEGLPCKWFAVPRS-SDKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGGHLHFEAYVQYE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 41152097 223 EYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKHLSD 265
Cdd:cd12264  80 EYDGFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-443 9.19e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 9.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 329 QRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQS----IRLIAELLSRAKAVKLREQEQKEEKLRLQQQE 404
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELAELEEELEELEEELEELEEELEEAE 350

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41152097 405 ERRRLQEAELRRVEEEKERALGLQRKERELRERLLSILL 443
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 326-436 1.12e-06

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: 52.05  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   326 EQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQ-- 403
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQem 548

                          90       100       110
                  ....*....|....*....|....*....|...
gi 41152097   404 EERRRLQEaELRRVEEEKERALGLQRKERELRE 436
Cdd:pfam17380 549 EERRRIQE-QMRKATEERSRLEAMEREREMMRQ 580
PTZ00121 PTZ00121
MAEBL; Provisional
 242-456 1.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   242 KGEDGKAVACNIKVSFDSTKHLSDAsiKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEK 321
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   322 LRKREQKQRDRELRRNQ--KKLEKLQAEEQKQLQEKIKL-EERKLLLAQ--RNLQSIRLIAELLSRAKAVK-------LR 389
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMalRKAEEAKKAEEARIEEVMKLyEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKkkveqlkKK 1641

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152097   390 EQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERElRERLLSILLSKKPDDSHTHDEL 456
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEEL 1707
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-439 1.58e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    329 QRDRELRRNQKKLEKLQAEE---QKQLQE-KIKLEERKLLLAQRNLQSIRLIAEL-LSRAKAVKLREQEQKEEKLRLQQQ 403
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIaelEKALAElRKELEELEEELEQLRKELEELSRQIsALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 41152097    404 EERRRL--QEAELRRVEEEKERALGLQRKERELRERLL 439
Cdd:TIGR02168  754 KELTELeaEIEELEERLEEAEEELAEAEAEIEELEAQI 791
RRM smart00360
RNA recognition motif;
170-240 2.33e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 39.88  E-value: 2.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152097    170 SEDVLVKVFEKFGEIRNVDIPmldpyREEMTGRnfhtfsfggHLNFeAYVQYREYMGFIQAMSALRGMKLM 240
Cdd:smart00360  12 TEEELRELFSKFGKVESVRLV-----RDKETGK---------SKGF-AFVEFESEEDAEKALEALNGKELD 67
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 345-433 5.14e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 345 QAEE--QKQLQEKIKLEE------RKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQ---QEERRRLQ--- 410
Cdd:cd16269 167 KAEEvlQEFLQSKEAEAEailqadQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErsyEEHLRQLKekm 246

                        90       100
                ....*....|....*....|...
gi 41152097 411 EAELRRVEEEKERALGLQRKERE 433
Cdd:cd16269 247 EEERENLLKEQERALESKLKEQE 269
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 170-240 2.68e-03

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 36.83  E-value: 2.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152097   170 SEDVLVKVFEKFGEIRNVDIPmldpyreemtgRNFHTFSFGghlnfEAYVQYREYMGFIQAMSALRGMKLM 240
Cdd:pfam00076  11 TEEDLKDLFSKFGPIKSIRLV-----------RDETGRSKG-----FAFVEFEDEEDAEKAIEALNGKELG 65
 
Name Accession Description Interval E-value
RRM_AKAP17A cd12264
RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar ...
 143-265 4.25e-81

RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins; This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409708 [Multi-domain]  Cd Length: 122  Bit Score: 252.96  E-value: 4.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 143 GERPDTIHLEGLPCKWFALKESgSEKPSEDVLVKVFEKFGEIRNVDIPMLDPYREEMTGRNFHTFSFGGHLNFEAYVQYR 222
Cdd:cd12264   1 GERPDTIHLEGLPCKWFAVPRS-SDKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGGHLHFEAYVQYE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 41152097 223 EYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKHLSD 265
Cdd:cd12264  80 EYDGFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-443 9.19e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 9.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 329 QRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQS----IRLIAELLSRAKAVKLREQEQKEEKLRLQQQE 404
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELAELEEELEELEEELEELEEELEEAE 350

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41152097 405 ERRRLQEAELRRVEEEKERALGLQRKERELRERLLSILL 443
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-472 3.93e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 3.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 269 KKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDRELRRNQKKLEKLQAEE 348
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 349 QKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQ 428
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41152097 429 RKERELRERLLSILLSKKPDDSHTHDELGVAHADLLQPVLDILQ 472
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 326-436 1.12e-06

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: 52.05  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   326 EQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQ-- 403
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQem 548

                          90       100       110
                  ....*....|....*....|....*....|...
gi 41152097   404 EERRRLQEaELRRVEEEKERALGLQRKERELRE 436
Cdd:pfam17380 549 EERRRIQE-QMRKATEERSRLEAMEREREMMRQ 580
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 330-438 1.40e-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: 51.49  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   330 RDRElrrNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRnLQSIRLIAELLSRAKA-VKLREQEQKE-EKLRLQQQEERR 407
Cdd:pfam15709 355 REQE---EQRRLQQEQLERAEKMREELELEQQRRFEEIR-LRKQRLEEERQRQEEEeRKQRLQLQAAqERARQQQEEFRR 430

                          90       100       110
                  ....*....|....*....|....*....|.
gi 41152097   408 RLQEAELRRVEEEKERALGLQRKERELRERL 438
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 274-456 7.32e-06

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: 49.35  E-value: 7.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   274 ERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQK----QRDRELRR-----NQKKLEKL 344
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQErmamERERELERirqeeRKRELERI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   345 QAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAE------LLSRAKAVKLREQEQKEEKLRLQQQEERRRlqeaELRRVE 418
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEaarkvkILEEERQRKIQQQKVEMEQIRAEQEEARQR----EVRRLE 441

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 41152097   419 EEKERALGLQRKERELRERLLSILLSKKPDDSHTHDEL 456
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 332-448 8.17e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 8.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 332 RELRRNQKKLEKLQAEEQkQLQEKIKLEERKLLLAQRNLQSIRL-IAELLSRAKAVKLREQEQKEEKLRLQQQ----EER 406
Cdd:COG1196 232 LKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDiarlEER 310

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 41152097 407 RRLQEAELRRVEEEKERALGLQRKERELRERLLSILLSKKPD 448
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
PTZ00121 PTZ00121
MAEBL; Provisional
 242-456 1.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   242 KGEDGKAVACNIKVSFDSTKHLSDAsiKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEK 321
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   322 LRKREQKQRDRELRRNQ--KKLEKLQAEEQKQLQEKIKL-EERKLLLAQ--RNLQSIRLIAELLSRAKAVK-------LR 389
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMalRKAEEAKKAEEARIEEVMKLyEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKkkveqlkKK 1641

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152097   390 EQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERElRERLLSILLSKKPDDSHTHDEL 456
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEEL 1707
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 269-446 1.20e-05

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: 48.58  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   269 KKRQLERQKLQELEQQREEQKR-REKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDRELRRNQKKLE----- 342
Cdd:pfam17380 325 RQAEMDRQAAIYAEQERMAMEReRELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEaarkv 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   343 KLQAEEQKQLQEKIKLEERKLLLAQRNLQSI---RLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEE 419
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQRevrRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR 484

                         170       180
                  ....*....|....*....|....*....
gi 41152097   420 EKERALGLQRK--ERELRERLLSILLSKK 446
Cdd:pfam17380 485 DRKRAEEQRRKilEKELEERKQAMIEEER 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 328-441 1.51e-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: 1.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 328 KQRDRELRRNQKKLEKLQAEEQKQLQE----KIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQ 403
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAElaelEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 41152097 404 EERRRLQEAELrrvEEEKERALGLQRKERELRERLLSI 441
Cdd:COG1196 315 EERLEELEEEL---AELEEELEELEEELEELEEELEEA 349
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-442 1.52e-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: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 305 KQKELEELERERKREEKLRKREQKQRdrelRRNQKKLEKLQAEEQKQLQEKIKLEERKL-LLAQRNLQSIRLIAELLSRA 383
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAELA 361

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41152097 384 KAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRERLLSIL 442
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 327-438 2.52e-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: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEER 406
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                        90       100       110
                ....*....|....*....|....*....|..
gi 41152097 407 RRLQEAELRRVEEEKERALGLQRKERELRERL 438
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREI 776
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-446 1.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 286 EEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDR---ELRRNQKKLEKLQAEEQKQLQEKIKLEERK 362
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEEL 353

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 363 LLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRERLLSIL 442
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433


                ....
gi 41152097 443 LSKK 446
Cdd:COG1196 434 EEEE 437
PTZ00121 PTZ00121
MAEBL; Provisional
 327-458 1.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLlaqRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEER 406
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41152097   407 RRLQEAELRRVEEEKERALGLqRKERELRERLLSILLSKKPDDSHTHDELGV 458
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEEL-KKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 327-441 1.33e-04

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: 44.75  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKL----------EERKLLLAQRN-LQSIR--------------------- 374
Cdd:COG4942  78 LAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqPPLALLLSPEDfLDAVRrlqylkylaparreqaeelra 157

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152097 375 -------LIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERAL-GLQRKERELRERLLSI 441
Cdd:COG4942 158 dlaelaaLRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaELQQEAEELEALIARL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-439 1.58e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    329 QRDRELRRNQKKLEKLQAEE---QKQLQE-KIKLEERKLLLAQRNLQSIRLIAEL-LSRAKAVKLREQEQKEEKLRLQQQ 403
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIaelEKALAElRKELEELEEELEQLRKELEELSRQIsALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 41152097    404 EERRRL--QEAELRRVEEEKERALGLQRKERELRERLL 439
Cdd:TIGR02168  754 KELTELeaEIEELEERLEEAEEELAEAEAEIEELEAQI 791
RRM smart00360
RNA recognition motif;
170-240 2.33e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 39.88  E-value: 2.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152097    170 SEDVLVKVFEKFGEIRNVDIPmldpyREEMTGRnfhtfsfggHLNFeAYVQYREYMGFIQAMSALRGMKLM 240
Cdd:smart00360  12 TEEELRELFSKFGKVESVRLV-----RDKETGK---------SKGF-AFVEFESEEDAEKALEALNGKELD 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 263-475 2.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 263 LSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQkeleelererkreeklrkREQKQRDRELRRNQKKLE 342
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA------------------EELLEALRAAAELAAQLE 403

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 343 KLQAEEQKQLQEKIKLEERKLLLAQRnlqsirlIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKE 422
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEA-------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41152097 423 RAlgLQRKERELRERLLSILLSKKPDDSHTHDELGVAHADLLQPVLDILQTVS 475
Cdd:COG1196 477 AA--LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 327-423 2.63e-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: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   327 QKQRDRELRRNQKKLEKLQ-AEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQ---Q 402
Cdd:pfam13868  84 EREQKRQEEYEEKLQEREQmDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkE 163

                          90       100
                  ....*....|....*....|.
gi 41152097   403 QEERRRLQEAELRRVEEEKER 423
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKER 184
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 327-432 2.64e-04

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: 41.95  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKL----------EERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEE 396
Cdd:pfam05672  26 QREREEQERLEKEEEERLRKEELRRRAEEERArreeearrleEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEE 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 41152097   397 KLRLQQQEERRRLQEAELRRVEEEKERalgLQRKER 432
Cdd:pfam05672 106 AEAKAREEAERQRQEREKIMQQEEQER---LERKKR 138
PTZ00121 PTZ00121
MAEBL; Provisional
 242-438 2.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   242 KGEDGKAVACNIKVSFDSTKHLSDAsiKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEK 321
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   322 LRKREQKQRDRELRRN---QKKLEKL-QAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAEL-----LSRAKAVKLREQE 392
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAaeaKKKADEAkKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeeLKKAEEKKKAEEA 1569

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152097   393 QKEEKLR---LQQQEERRRLQEA------------------ELRRVEEEKERALGLqRKERELRERL 438
Cdd:PTZ00121 1570 KKAEEDKnmaLRKAEEAKKAEEArieevmklyeeekkmkaeEAKKAEEAKIKAEEL-KKAEEEKKKV 1635
PTZ00121 PTZ00121
MAEBL; Provisional
 242-433 4.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   242 KGEDGKAVACNIKVSFDSTKHLSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEK 321
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   322 LRKREQKQRDRELRRNQKKLEKLQAEE-QKQLQEKIKLEE-RKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLR 399
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475

                         170       180       190
                  ....*....|....*....|....*....|....
gi 41152097   400 LQQQEERRRLQEAElRRVEEEKERALGLQRKERE 433
Cdd:PTZ00121 1476 KKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEA 1508
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 345-433 5.14e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 345 QAEE--QKQLQEKIKLEE------RKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQ---QEERRRLQ--- 410
Cdd:cd16269 167 KAEEvlQEFLQSKEAEAEailqadQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErsyEEHLRQLKekm 246

                        90       100
                ....*....|....*....|...
gi 41152097 411 EAELRRVEEEKERALGLQRKERE 433
Cdd:cd16269 247 EEERENLLKEQERALESKLKEQE 269
PRK12704 PRK12704
phosphodiesterase; Provisional
 328-436 6.58e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097  328 KQRDRELRRNQKKLekLQAEEQ-KQLQEKIKLEERKLLLAQRNLQsiRLIAELLSRAKAVKLREQEQKEEKLR---LQQQ 403
Cdd:PRK12704  78 RERRNELQKLEKRL--LQKEENlDRKLELLEKREEELEKKEKELE--QKQQELEKKEEELEELIEEQLQELERisgLTAE 153

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41152097  404 EERRRLqeaeLRRVEEE--KERALGLQRKERELRE 436
Cdd:PRK12704 154 EAKEIL----LEKVEEEarHEAAVLIKEIEEEAKE 184
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
329-437 7.08e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 7.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 329 QRDRELRRNQKKleklQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLS-RAKAV---KLREQEQKEEKLRLQQQE 404
Cdd:COG2268 209 ERETEIAIAQAN----REAEEAELEQEREIETARIAEAEAELAKKKAEERREAeTARAEaeaAYEIAEANAEREVQRQLE 284

                        90       100       110
                ....*....|....*....|....*....|...
gi 41152097 405 ERRRLQEAELRRVEEEKERAlglqRKERELRER 437
Cdd:COG2268 285 IAEREREIELQEKEAEREEA----ELEADVRKP 313
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 387-437 9.60e-04

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: 40.41  E-value: 9.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 41152097   387 KLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRER 437
Cdd:pfam05672  22 QAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR 72
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 328-437 9.72e-04

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: 41.23  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   328 KQRDRElrrnqkklEKLQAEEQKQLQEKIKLEERKLL----------------LAQRNLQSIRLIAELLSRAKAVKLREQ 391
Cdd:pfam13904  64 KQRQRQ--------KELQAQKEEREKEEQEAELRKRLakekyqewlqrkarqqTKKREESHKQKAAESASKSLAKPERKV 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 41152097   392 EQKEEKLRLQQQeERRRLQEAELRRVEEEKERalglQRKERELRER 437
Cdd:pfam13904 136 SQEEAKEVLQEW-ERKKLEQQQRKREEEQREQ----LKKEEEEQER 176
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 390-436 1.04e-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: 40.81  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 41152097   390 EQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRE 436
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEE 47
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 335-431 1.31e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 40.32  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097  335 RRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEeklrlqqqEERRRLQEAEL 414
Cdd:PRK07352  50 ERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEKQAI--------EDMARLKQTAA 121

                         90
                 ....*....|....*..
gi 41152097  415 RRVEEEKERALGLQRKE 431
Cdd:PRK07352 122 ADLSAEQERVIAQLRRE 138
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 327-439 1.48e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   327 QKQRDR-ELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQR---NLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQ 402
Cdd:pfam13868 146 EKEEEReEDERILEYLKEKAEREEEREAEREEIEEEKEREIARlraQQEKAQDEKAERDELRAKLYQEEQERKERQKERE 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 41152097   403 QEERRRLQEAELRRVEEE----KERALGLQRK-ERELRERLL 439
Cdd:pfam13868 226 EAEKKARQRQELQQAREEqielKERRLAEEAErEEEEFERML 267
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 170-256 1.84e-03

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 37.26  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 170 SEDVLVKVFEKFGEIRNVDIpmldPYREEMTGRNFhtfsfgghlnfeAYVQYREYMGFIQAMSALRGMKLmykgeDGKav 249
Cdd:cd00590  11 TEEDLRELFSKFGEVVSVRI----VRDRDGKSKGF------------AFVEFESPEDAEKALEALNGTEL-----GGR-- 67


                ....*..
gi 41152097 250 acNIKVS 256
Cdd:cd00590  68 --PLKVS 72
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 329-437 1.96e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 39.22  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   329 QRDRELRRNQKK-----LEKLQAE---EQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLS-----RAKAVKLREQEQKE 395
Cdd:TIGR02473   5 QKLLDLREKEEEqakleLAKAQAEferLETQLQQLIKYREEYEQQALEKVGAGTSALELSNyqrfiRQLDQRIQQQQQEL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 41152097   396 EKLRLQQQEERRRLQEA--ELRRVEEEKERALGLQRKERELRER 437
Cdd:TIGR02473  85 ALLQQEVEAKRERLLEArrELKALEKLKEKKQKEYRAEEAKREQ 128
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
327-438 2.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097  327 QKQRDRELRR-------NQKKLEKLQAEEQKQLQEKIKLEER--KLLLAQRNLQSIRLIAELLS---------RAKAVKL 388
Cdd:COG4913  591 EKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERleALEAELDALQERREALQRLAeyswdeidvASAEREI 670

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152097  389 REQEQKEEKLR-----LQQQEERRRLQEAELRRVEEEKERalgLQRKERELRERL 438
Cdd:COG4913  671 AELEAELERLDassddLAALEEQLEELEAELEELEEELDE---LKGEIGRLEKEL 722
PRK12704 PRK12704
phosphodiesterase; Provisional
 339-441 2.18e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097  339 KKLEKLQAEEQKQLQEKIkLEErklllAQRNLQSIRLIAELLSRAKAVKLR---EQEQKEEKLRLQQQEERRRLQEAELR 415
Cdd:PRK12704  26 KKIAEAKIKEAEEEAKRI-LEE-----AKKEAEAIKKEALLEAKEEIHKLRnefEKELRERRNELQKLEKRLLQKEENLD 99

                         90       100
                 ....*....|....*....|....*.
gi 41152097  416 RVEEEkeralgLQRKERELRERLLSI 441
Cdd:PRK12704 100 RKLEL------LEKREEELEKKEKEL 119
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 328-424 2.22e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.36  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   328 KQRDRELRRNQKKLEKLqAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERR 407
Cdd:pfam20492  23 KKAQEELEESEETAEEL-EEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVER 101

                          90
                  ....*....|....*..
gi 41152097   408 RlqEAELRRVEEEKERA 424
Cdd:pfam20492 102 K--EEEARRLQEELEEA 116
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 327-437 2.37e-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: 40.67  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   327 QKQRDRELRRNQKKLEKLQA--------EEQKQLQEKIKLEERKLLLA--QRNLQSIRLIAELLSRAKAVKLREQEQKEE 396
Cdd:pfam13868  58 EEEEEKEEERKEERKRYRQEleeqieerEQKRQEEYEEKLQEREQMDEivERIQEEDQAEAEEKLEKQRQLREEIDEFNE 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 41152097   397 KLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRER 437
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI 178
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 328-435 2.52e-03

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: 38.87  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   328 KQRDRELRRNQKKLEKLQAEEQKQlQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERR 407
Cdd:pfam05672  19 KRRQAREQREREEQERLEKEEEER-LRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQE 97

                          90       100       110
                  ....*....|....*....|....*....|.
gi 41152097   408 RLQ---EAELRRVEEEKERalglQRKERELR 435
Cdd:pfam05672  98 RLQkqkEEAEAKAREEAER----QRQEREKI 124
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 170-240 2.68e-03

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 36.83  E-value: 2.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152097   170 SEDVLVKVFEKFGEIRNVDIPmldpyreemtgRNFHTFSFGghlnfEAYVQYREYMGFIQAMSALRGMKLM 240
Cdd:pfam00076  11 TEEDLKDLFSKFGPIKSIRLV-----------RDETGRSKG-----FAFVEFEDEEDAEKAIEALNGKELG 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 327-426 2.74e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEER 406
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749

                        90       100       110
                ....*....|....*....|....*....|..
gi 41152097 407 RRL------------QEAELRRVEEEKERaLG 426
Cdd:COG1196 750 EEAleelpeppdleeLERELERLEREIEA-LG 780
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 327-416 3.08e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKL----EERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQ 402
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                        90
                ....*....|....
gi 41152097 403 QEERRRLQEAELRR 416
Cdd:COG4942 228 LIARLEAEAAAAAE 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
328-438 3.73e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097  328 KQRDRELRRNQKKLEKLQAEEQKQLQEKiKLEERKLLLAQRNLQSIRLIAELLSRAKA--VKLREQEQKEEKlRLQQQEE 405
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEEL-KKEIEELEEKVKELKELKEKAEEYIKLSEfyEEYLDELREIEK-RLSRLEE 321

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41152097  406 RRRLQEAELRRVEEEKERALGLQRKERELRERL 438
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRL 354
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 183-456 4.13e-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: 40.73  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    183 EIRNVDIPMLDPYREEMTGRNFHTFSFGGHLNFEAYVQYREYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKH 262
Cdd:pfam02463  597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    263 LSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQR-----DRELRRN 337
Cdd:pfam02463  677 EIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKideeeEEEEKSR 756

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    338 QKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQ-----SIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEA 412
Cdd:pfam02463  757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEekeekLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 41152097    413 ELRR--VEEEKERALGLQRKERELRERLLSILLSKKPDDSHTHDEL 456
Cdd:pfam02463  837 ELALelKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
PTZ00121 PTZ00121
MAEBL; Provisional
 242-456 4.25e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   242 KGEDGKAVACNIKVSFDSTKHLSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEK 321
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   322 LRKREQKQRDRELRRnqKKLEKLQAEE-QKQLQEKIKLEE-RKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLR 399
Cdd:PTZ00121 1424 KKKAEEKKKADEAKK--KAEEAKKADEaKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152097   400 LQQQEERRRLQEaELRRVEEEKERALGLQRKERELRERLLSILLSKKPDDSHTHDEL 456
Cdd:PTZ00121 1502 AKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
320-424 4.32e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 4.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 320 EKLRKREQKQRDRELR--RNQKKLEKLQAEE-QKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAVKLreQEQKEE 396
Cdd:COG2268 223 AEEAELEQEREIETARiaEAEAELAKKKAEErREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIEL--QEKEAE 300

                        90       100
                ....*....|....*....|....*...
gi 41152097 397 KLRLQQQEERRRLQEAELRRVEEEkERA 424
Cdd:COG2268 301 REEAELEADVRKPAEAEKQAAEAE-AEA 327
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 337-433 4.45e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   337 NQKKLEKLQAEE--QKQLQEKIKLEE------RKLLLAQRNLQSIRLIAELLSRAKAV---KLREQEQKEEKLRLQQQEE 405
Cdd:pfam02841 165 NQVPRKGVKAEEvlQEFLQSKEAVEEailqtdQALTAKEKAIEAERAKAEAAEAEQELlreKQKEEEQMMEAQERSYQEH 244

                          90       100       110
                  ....*....|....*....|....*....|.
gi 41152097   406 RRRLQ---EAELRRVEEEKERALGLQRKERE 433
Cdd:pfam02841 245 VKQLIekmEAEREQLLAEQERMLEHKLQEQE 275
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-442 5.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 5.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097  332 RELRRNQKKLEKLQAEEQKQLQEKIKLEerKLLLAQRNLQSIRLIAELL----SRAKAVKLREQEQKEEKLRLQQQE--- 404
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELE--KVLKKESELIKLKELAEQLkeleEKLKKYNLEELEKKAEEYEKLKEKlik 536

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 41152097  405 ---ERRRLQEaELRRVEEEKERALGLQRKERELRERLLSIL 442
Cdd:PRK03918 537 lkgEIKSLKK-ELEKLEELKKKLAELEKKLDELEEELAELL 576
PTZ00121 PTZ00121
MAEBL; Provisional
 242-436 5.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   242 KGEDGKAVACNIKVSFDSTKHLSDASIK---KRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKR 318
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   319 EEKLRKREQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLiAELLSRAKAVKLREQEQKEEKL 398
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADELKKAEEL 1557

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 41152097   399 RlqQQEERRRLQEAelRRVEEEKERALglqRKERELRE 436
Cdd:PTZ00121 1558 K--KAEEKKKAEEA--KKAEEDKNMAL---RKAEEAKK 1588
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 328-431 5.31e-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: 40.04  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    328 KQRDRELRRNQKKLEKLQ---AEEQKQLQEK-IKLEERKLLLAQRNLQSIRLIAELLS---RAKAVKLREQEQKEEKLRL 400
Cdd:TIGR02168  235 EELREELEELQEELKEAEeelEELTAELQELeEKLEELRLEVSELEEEIEELQKELYAlanEISRLEQQKQILRERLANL 314

                           90       100       110
                   ....*....|....*....|....*....|.
gi 41152097    401 QQQEERRRLQEAELRRVEEEKERALGLQRKE 431
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEK 345
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 266-463 5.37e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 5.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 266 ASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDRELRRNQKKLEKLQ 345
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 346 AEEQKQLQEKIKL----------EERKLLLAQRN-LQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAEL 414
Cdd:COG4942  97 AELEAQKEELAELlralyrlgrqPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41152097 415 RRVEEEKERALGLQRKERELRERLLSILLSKKPDDSHTHDELGVAHADL 463
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
332-445 5.86e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 332 RELRRNQKKLEKLQAEEQKQLQEK----IKL-EERKLLLAQRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQEER 406
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTPNhpdvIALrAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41152097 407 RRLQEAELRRveeekeralgLQRkERELRERLLSILLSK 445
Cdd:COG3206 346 LPELEAELRR----------LER-EVEVARELYESLLQR 373
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 335-438 7.16e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 37.72  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   335 RRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELlSRAKAVKLREQEQKEEKLRLQQQEERRRLQEAEL 414
Cdd:pfam15346  14 RRVEEAVAKRVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEEL-EREREAELEEERRKEEEERKKREELERILEENNR 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 41152097   415 ------RRVEEEKERALGLQRKERELRERL 438
Cdd:pfam15346  93 kieeaqRKEAEERLAMLEEQRRMKEERQRR 122
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 327-436 7.40e-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: 39.67  E-value: 7.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097    327 QKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKAV--KLREQEQKEEKLRLQQQE 404
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKalEIKKQEWKLEQLAADLSK 466

                           90       100       110
                   ....*....|....*....|....*....|....
gi 41152097    405 ERRRLQ--EAELRRVEEEkeralgLQRKERELRE 436
Cdd:TIGR02169  467 YEQELYdlKEEYDRVEKE------LSKLQRELAE 494
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 332-528 7.89e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 332 RELRRNQKKLEKLQaEEQKQLQEKI-----KLEERKLLLAQRN---------------LQSIRLIAELLSRAKAVK---- 387
Cdd:COG3883  51 EEYNELQAELEALQ-AEIDKLQAEIaeaeaEIEERREELGERAralyrsggsvsyldvLLGSESFSDFLDRLSALSkiad 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 388 -----LREQ-------EQKEEKLRLQQQEERRRLQEAE-----LRRVEEEKERAL-GLQRKERELRERLLSILLSKKPDD 449
Cdd:COG3883 130 adadlLEELkadkaelEAKKAELEAKLAELEALKAELEaakaeLEAQQAEQEALLaQLSAEEAAAEAQLAELEAELAAAE 209

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152097 450 shthDELGVAHADLLQPVLDILQTVSSGCVSATTLHPLGGQPPAGAPKESPAHPEADGAPKSVNGSVAEEAPCKEVQSS 528
Cdd:COG3883 210 ----AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 332-446 7.94e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 7.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 332 RELRRNQKKLEKLQAEEQKQLQEkIKLEerklllaqrnlqsirlIAELLSRAKAvklrEQEQKEEKLRLQQQEERRRLQE 411
Cdd:cd06503  40 EEAEKAKEEAEELLAEYEEKLAE-ARAE----------------AQEIIEEARK----EAEKIKEEILAEAKEEAERILE 98

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 41152097 412 AELRRVEEEKERALglqrkeRELRERL--LSILLSKK 446
Cdd:cd06503  99 QAKAEIEQEKEKAL------AELRKEVadLAVEAAEK 129
PTZ00121 PTZ00121
MAEBL; Provisional
 327-436 8.67e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   327 QKQRDRELRRNQkklEKLQAEEQKQLQEKIKLEE--------RKLLLAQRNLQSIRLIAELLSRA--KAVKLREQEQKEE 396
Cdd:PTZ00121 1276 EARKADELKKAE---EKKKADEAKKAEEKKKADEakkkaeeaKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEA 1352

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 41152097   397 KLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRE 436
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
PTZ00121 PTZ00121
MAEBL; Provisional
 233-438 9.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   233 ALRGMKLMYKGEdgKAVACNIKVSFDSTKHLSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAeeRKQkeleel 312
Cdd:PTZ00121 1579 ALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE--KKK------ 1648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   313 ererkreeklrkREQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKlllAQRNLQSIRLIAELLSRAKAVKLREQE 392
Cdd:PTZ00121 1649 ------------AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED---EKKAAEALKKEAEEAKKAEELKKKEAE 1713

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 41152097   393 QKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRERL 438
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
331-438 9.55e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 9.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097 331 DRELRRNQKKLEKLQaEEQKQLQEKIK-LEERKLLLAQRNLQSIRLIAELlsrakavklreqeqkEEKLRLQQQEERRRL 409
Cdd:COG2433 398 EREKEHEERELTEEE-EEIRRLEEQVErLEAEVEELEAELEEKDERIERL---------------ERELSEARSEERREI 461

                        90       100       110
                ....*....|....*....|....*....|
gi 41152097 410 Q-EAELRRVEEEKERalgLQRKERELRERL 438
Cdd:COG2433 462 RkDREISRLDREIER---LERELEEERERI 488
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 330-421 9.65e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152097   330 RDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKlllaqRNLQSIRLIAELLSRAKAVKLREQEQKEEKLRLQQQE--ERR 407
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-----NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlkETI 435

                          90
                  ....*....|....
gi 41152097   408 RLQEAELRRVEEEK 421
Cdd:TIGR04523 436 IKNNSEIKDLTNQD 449
 
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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