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Conserved domains on  [gi|32565466|ref|NP_872036|]
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FIP-RBD domain-containing protein [Caenorhabditis elegans]

Protein Classification

coiled-coil domain-containing protein; kinesin family protein( domain architecture ID 1006538)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership| kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-227 1.28e-07

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      7 SEEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK 86
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     87 REKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQ- 165
Cdd:TIGR02168  331 KLDELAEEL-----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERl 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565466    166 --DIDSSSEMVEVLALETEELRRKVDGPRSESISDR-EDMHEEIEILKAKVAELMKEKEEMTDQL 227
Cdd:TIGR02168  406 eaRLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREEL 470
RBD-FIP super family cl09694
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 256-292 2.49e-05

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


The actual alignment was detected with superfamily member pfam09457:

Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 41.17  E-value: 2.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 32565466   256 QLLDALREQEICNQKLRVYINGILMRVIERHPEILEI 292
Cdd:pfam09457   4 ELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEV 40
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-227 1.28e-07

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: 53.91  E-value: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      7 SEEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK 86
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     87 REKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQ- 165
Cdd:TIGR02168  331 KLDELAEEL-----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERl 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565466    166 --DIDSSSEMVEVLALETEELRRKVDGPRSESISDR-EDMHEEIEILKAKVAELMKEKEEMTDQL 227
Cdd:TIGR02168  406 eaRLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREEL 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 17-265 3.33e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  17 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESw 96
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  97 nlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 176
Cdd:COG1196 305 ----ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 177 LALETEELRRKVDGpRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 256
Cdd:COG1196 381 LEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459


                ....*....
gi 32565466 257 LLDALREQE 265
Cdd:COG1196 460 ALLELLAEL 468
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 34-229 3.03e-06

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 49.26  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    34 SLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETeswnlkyqmLEKDLISVKKD 113
Cdd:pfam05667 280 LLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE---------LQEQLEDLESS 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   114 AERSNEETKRIRNELEKTENKLEEaqllvegMEEERIQLERQFRKFK-------------EEAQQDIDSSSEMVEVLALE 180
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEE-------LKEQNEELEKQYKVKKktldllpdaeeniAKLQALVDASAQRLVELAGQ 423

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 32565466   181 TEELR-------RKVDGPRSESISDREDMHEEIEILKAK---VAELMKEKEEMTDQLLA 229
Cdd:pfam05667 424 WEKHRvplieeyRALKEAKSNKEDESQRKLEEIKELREKikeVAEEAKQKEELYKQLVA 482
PTZ00121 PTZ00121
MAEBL; Provisional
 4-227 4.81e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     4 EFVSEEESKYAMNQLNSFTKRYSElEERNMSLSDERTRLKTENSVLKERMHNLEEQltdNEDRFKQLLSDEKARGTESMS 83
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAE-EDKNMALRKAEEAKKAEEARIEEVMKLYEEE---KKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    84 RLKREKELETESWNLKYQMLEKDLISVKKDAE----------RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLE 153
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkikaaeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565466   154 rQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEeieilKAKVAELMKEKEEMTDQL 227
Cdd:PTZ00121 1706 -ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEI 1773
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 256-292 2.49e-05

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 41.17  E-value: 2.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 32565466   256 QLLDALREQEICNQKLRVYINGILMRVIERHPEILEI 292
Cdd:pfam09457   4 ELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEV 40
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-227 1.28e-07

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: 53.91  E-value: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      7 SEEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK 86
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     87 REKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQ- 165
Cdd:TIGR02168  331 KLDELAEEL-----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERl 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565466    166 --DIDSSSEMVEVLALETEELRRKVDGPRSESISDR-EDMHEEIEILKAKVAELMKEKEEMTDQL 227
Cdd:TIGR02168  406 eaRLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREEL 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-216 2.37e-07

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: 53.14  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLlsdeKARGTESMSRLKR 87
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL----REALDELRAELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     88 EKELETESWNlKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfKEEAQQDI 167
Cdd:TIGR02168  815 LNEEAANLRE-RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEAL 889

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 32565466    168 DSSSEMVEVLALETEELRRKVDGPRSESISDRE---DMHEEIEILKAKVAEL 216
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREklaQLELRLEGLEVRIDNL 941
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 17-265 3.33e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  17 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESw 96
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  97 nlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 176
Cdd:COG1196 305 ----ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 177 LALETEELRRKVDGpRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 256
Cdd:COG1196 381 LEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459


                ....*....
gi 32565466 257 LLDALREQE 265
Cdd:COG1196 460 ALLELLAEL 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-271 7.47e-07

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: 51.60  E-value: 7.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     38 ERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDekargTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERS 117
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE-----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    118 NEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDG-----PR 192
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERlesleRR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    193 SESISDR--------EDMHEEIEILKAKVAELMKEKEEMTDQL-----LATSVERGRSLIADTPSLADELAGGDSSQLLD 259
Cdd:TIGR02168  833 IAATERRledleeqiEELSEDIESLAAEIEELEELIEELESELeallnERASLEEALALLRSELEELSEELRELESKRSE 912

                          250
                   ....*....|..
gi 32565466    260 ALREQEICNQKL 271
Cdd:TIGR02168  913 LRRELEELREKL 924
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-249 1.90e-06

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: 50.07  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK- 86
Cdd:TIGR02169  222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEa 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     87 ---------REKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQllvEGMEEERIQLERQFR 157
Cdd:TIGR02169  302 eiaslersiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---EELEDLRAELEEVDK 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    158 KFKeEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESI---SDREDMHEEIEILKAKVAELMKEKEEMTDQlLATSVER 234
Cdd:TIGR02169  379 EFA-ETRDELKDYREKLEKLKREINELKRELDRLQEELQrlsEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWK 456

                          250
                   ....*....|....*
gi 32565466    235 GRSLIADTPSLADEL 249
Cdd:TIGR02169  457 LEQLAADLSKYEQEL 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-266 2.57e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrlKR 87
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----LE 319

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  88 EKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKF---KEEAQ 164
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAlraAAELA 399

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 165 QDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTdQLLATSVERGRSLIADTPS 244
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE-ALLELLAELLEEAALLEAA 478

                       250       260
                ....*....|....*....|..
gi 32565466 245 LADELAGGDSSQLLDALREQEI 266
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAE 500
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 34-229 3.03e-06

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 49.26  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    34 SLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETeswnlkyqmLEKDLISVKKD 113
Cdd:pfam05667 280 LLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE---------LQEQLEDLESS 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   114 AERSNEETKRIRNELEKTENKLEEaqllvegMEEERIQLERQFRKFK-------------EEAQQDIDSSSEMVEVLALE 180
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEE-------LKEQNEELEKQYKVKKktldllpdaeeniAKLQALVDASAQRLVELAGQ 423

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 32565466   181 TEELR-------RKVDGPRSESISDREDMHEEIEILKAK---VAELMKEKEEMTDQLLA 229
Cdd:pfam05667 424 WEKHRvplieeyRALKEAKSNKEDESQRKLEEIKELREKikeVAEEAKQKEELYKQLVA 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 16-250 4.59e-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: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  16 NQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETES 95
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  96 WNLKYQMLEkdlisvkkdAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVE 175
Cdd:COG1196 382 EELAEELLE---------ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565466 176 VLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELA 250
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
PTZ00121 PTZ00121
MAEBL; Provisional
 4-227 4.81e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     4 EFVSEEESKYAMNQLNSFTKRYSElEERNMSLSDERTRLKTENSVLKERMHNLEEQltdNEDRFKQLLSDEKARGTESMS 83
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAE-EDKNMALRKAEEAKKAEEARIEEVMKLYEEE---KKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    84 RLKREKELETESWNLKYQMLEKDLISVKKDAE----------RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLE 153
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkikaaeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565466   154 rQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEeieilKAKVAELMKEKEEMTDQL 227
Cdd:PTZ00121 1706 -ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEI 1773
mukB PRK04863
chromosome partition protein MukB;
50-169 1.02e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.03  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    50 KERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRL----KREKELETEswnlkYQMLEKDLISVKkDAERSNEETKR 123
Cdd:PRK04863  279 NERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELaelnEAESDLEQD-----YQAASDHLNLVQ-TALRQQEKIER 352

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 32565466   124 IRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfKEEAQQDIDS 169
Cdd:PRK04863  353 YQADLEELEERLEEQNEVVEEADEQQEENEAR----AEAAEEEVDE 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-262 1.49e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrlKR 87
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-----LE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  88 EKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfKEEAQQDI 167
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE----LEELEEAL 430

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 168 DSSSEMVEVLALETEELRRKvdgpRSESISDREDMHEEIEILKAKVAELMKEKEEmTDQLLATSVERGRSLIADTPSLAD 247
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEE----EAELEEEEEALLELLAELLEEAALLEAALAE-LLEELAEAAARLLLLLEAEADYEG 505

                       250
                ....*....|....*
gi 32565466 248 ELAGGDSSQLLDALR 262
Cdd:COG1196 506 FLEGVKAALLLAGLR 520
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-218 1.54e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    6 VSEEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKE---RMHNLEEQLTDNEDRFKQLLSDEKARGTESM 82
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESV 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   83 SRLKRE-KELEteswnlKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK- 160
Cdd:PRK03918 588 EELEERlKELE------PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEy 661

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 32565466  161 EEAQQDIDSSSEMVEVLALETEELRRKVDgprsESISDREDMHEEIEILKAKVAELMK 218
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRRE----EIKKTLEKLKEELEEREKAKKELEK 715
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 51-169 1.65e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.25  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   51 ERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRLK----REKELETEswnlkYQMLEKDLISVKkDAERSNEETKRI 124
Cdd:COG3096  279 ERRELSERALELRRELFgaRRQLAEEQYRLVEMARELEelsaRESDLEQD-----YQAASDHLNLVQ-TALRQQEKIERY 352

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 32565466  125 RNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQDIDS 169
Cdd:COG3096  353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARL----EAAEEEVDS 393
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 256-292 2.49e-05

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 41.17  E-value: 2.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 32565466   256 QLLDALREQEICNQKLRVYINGILMRVIERHPEILEI 292
Cdd:pfam09457   4 ELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEV 40
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 23-168 2.97e-05

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: 44.92  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  23 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKargtESMSRLKREKELETESWNLK-YQ 101
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEQLGNVRNNKeYE 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32565466 102 MLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDID 168
Cdd:COG1579  93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
24-220 1.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   24 RYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLS-DEKARGTESMSRLKRE---KELETESWNLK 99
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElKEKAEEYIKLSEFYEEyldELREIEKRLSR 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  100 YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLAL 179
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 32565466  180 ETEELRRKvdgpRSESISDREDMHEEIEILKAKVAELMKEK 220
Cdd:PRK03918 399 AKEEIEEE----ISKITARIGELKKEIKELKKAIEELKKAK 435
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 24-156 1.76e-04

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 41.52  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    24 RYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDnedrFKQLLSDEKARGTESmsrlkrekeletESWNLKYQML 103
Cdd:pfam12718  22 KVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKE----AKEKAEESEKLKTNN------------ENLTRKIQLL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 32565466   104 EKDLisvkkdaERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQF 156
Cdd:pfam12718  86 EEEL-------EESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKY 131
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-272 2.24e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  66 RFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGM 145
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 146 EEERIQLERQfrkfKEEAQQDIDSSSEMVEVLALETEELRRKvdgprsesisdREDMHEEIEILKAKVAELMKEKEEMTD 225
Cdd:COG1196 294 LAELARLEQD----IARLEERRRELEERLEELEEELAELEEE-----------LEELEEELEELEEELEEAEEELEEAEA 358

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 32565466 226 QLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQEICNQKLR 272
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLE 403
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-251 2.84e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   10 ESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLlsdekargtESMSRLKREK 89
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL---------EELKEEIEEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   90 ELETESWNLKYQMLEKDLisvkKDAERSNEETKRIRNELEKTENKLEEaqllVEGMEEERIQLERQFRKFKEEAQQdids 169
Cdd:PRK03918 244 EKELESLEGSKRKLEEKI----RELEERIEELKKEIEELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELRE---- 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  170 ssemVEVLALETEELRRKVDgprsESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLAtsVERGRSLIADTPSLADEL 249
Cdd:PRK03918 312 ----IEKRLSRLEEEINGIE----ERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEAKAKKEELERLKKRL 381


                 ..
gi 32565466  250 AG 251
Cdd:PRK03918 382 TG 383
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 8-198 2.91e-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: 42.83  E-value: 2.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLsdekaRGTESMSRLKR 87
Cdd:COG4942  47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPP 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  88 EKEL-ETESWNLKYQMLE-------------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLE 153
Cdd:COG4942 122 LALLlSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32565466 154 RQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISD 198
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 30-166 3.10e-04

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: 43.02  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    30 ERNMSLSDERTRLKTENSVLKERMH---NLEEQLTDNEDRF-KQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEK 105
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMReelELEQQRRFEEIRLrKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRR 430

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32565466   106 DLISVK-----KDAERSNEETKRiRNELEktENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQD 166
Cdd:pfam15709 431 KLQELQrkkqqEEAERAEAEKQR-QKELE--MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLE 493
PTZ00121 PTZ00121
MAEBL; Provisional
 7-236 4.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     7 SEEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmsRLK 86
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK--KKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    87 REKELETESWNLKYQMLEKDLISVKKDAE--RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQ 164
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32565466   165 QDidsssemVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKaKVAELMKEKEEMTDQLLATSVERGR 236
Cdd:PTZ00121 1730 IK-------AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK-KAEEIRKEKEAVIEEELDEEDEKRR 1793
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 42-272 5.22e-04

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 41.55  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    42 LKTENSVLKERMHNLEEQLTDNEDRFKQLL----------------SDEKARGTESMSRLKREKELETESWNLKYQMLEK 105
Cdd:pfam04849  92 LLKQNSVLTERNEALEEQLGSAREEILQLRhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   106 DLISVKKDAERSNEETKRIRNELEKTENKleEAQLLVEGMEEERiqlerqfrkfkeEAQQDIdssSEMVEVLALETEELR 185
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEK--EQQLMSDCVEQLS------------EANQQM---AELSEELARKMEENL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   186 RKvdgprsesisdredmHEEIEILKAKVAEL-------MKEKEEMTdQLLATSVERGRSLIADTPSLADELAggdssQLL 258
Cdd:pfam04849 235 RQ---------------QEEITSLLAQIVDLqhkckelGIENEELQ-QHLQASKEAQRQLTSELQELQDRYA-----ECL 293

                         250
                  ....*....|....
gi 32565466   259 DALREQEICNQKLR 272
Cdd:pfam04849 294 GMLHEAQEELKELR 307
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-227 5.75e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  49 LKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNEL 128
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 129 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEE 205
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                       170       180
                ....*....|....*....|..
gi 32565466 206 IEILKAKVAELMKEKEEMTDQL 227
Cdd:COG1196 378 EEELEELAEELLEALRAAAELA 399
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 8-189 6.13e-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: 42.03  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     8 EEESKYAMNQLNSFTKRYSELEErnmSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrLKR 87
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE----LEK 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    88 EKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDI 167
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561

                         170       180
                  ....*....|....*....|..
gi 32565466   168 DSSSEMVEVLALETEELRRKVD 189
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVE 583
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-266 6.47e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   49 LKERMHNLEEQLTDNEDRFKQLlsdEKARGTESMSRLKREKELETESWNLKYQMLEKDLisvkKDAERSNEETKRIRNEL 128
Cdd:COG4913  622 LEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQL 694

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  129 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEV-LALETEELRRKVDGPRSESiSDREDMHE 204
Cdd:COG4913  695 EELEAELEELEEELDELKGEIGRLEKELEQAEEEldeLQDRLEAAEDLARLeLRALLEERFAAALGDAVER-ELRENLEE 773

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32565466  205 EIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggdssqLLDALREQEI 266
Cdd:COG4913  774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA------LLDRLEEDGL 829
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 99-212 8.31e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.87  E-value: 8.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  99 KYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLA 178
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208

                        90       100       110
                ....*....|....*....|....*....|....
gi 32565466 179 LETEELRRKVDGPRSESISDREDMHEEIEILKAK 212
Cdd:COG4026 209 LEVFSLEELWKELFPEELPEEDFIYFATENLKPG 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 86-227 8.83e-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: 41.58  E-value: 8.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     86 KREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQ 165
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALAN 295

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565466    166 DIDSSSEMVEVLALETEELRRK---VDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 227
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 6-227 9.14e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 9.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      6 VSEEESKYAMnQLNSFTKRYSELEERnmslsdeRTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSdEKARGTESMSRL 85
Cdd:pfam01576   38 LCEEKNALQE-QLQAETELCAEAEEM-------RARLAARKQELEEILHELESRLEEEEERSQQLQN-EKKKMQQHIQDL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     86 K---------REK-ELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllvegmEEERIQLERQ 155
Cdd:pfam01576  109 EeqldeeeaaRQKlQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAE--------EEEKAKSLSK 180

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32565466    156 FRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAelmKEKEEMTDQL 227
Cdd:pfam01576  181 LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA---KKEEELQAAL 249
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 115-222 9.86e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 9.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  115 ERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRK----FKEEAQQDIDSSSEMVEVLALETEELRRKVDG 190
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlleeAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602

                         90       100       110
                 ....*....|....*....|....*....|....
gi 32565466  191 P--RSESISDREDMHEEIEILKAKVAELMKEKEE 222
Cdd:PRK00409 603 SvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 27-210 1.39e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     27 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK---QLLSDEKARGTESMSRLKREKELETESWNLKYQmL 103
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK-L 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    104 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRkfkeEAQQDIdssSEMVEVLALETee 183
Cdd:pfam01576  214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQI---SELQEDLESER-- 284

                          170       180
                   ....*....|....*....|....*..
gi 32565466    184 lrrkvdGPRSESISDREDMHEEIEILK 210
Cdd:pfam01576  285 ------AARNKAEKQRRDLGEELEALK 305
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 19-223 1.83e-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: 40.49  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    19 NSFTKRYSELEERNMSLSDERTRLKTENsVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrLKREKELETESWNL 98
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQERLRQEKEEKAREVERRRKLEEAEKARQAE----MDRQAAIYAEQERM 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    99 kyqmlekdlisvkkdAERSNEETKRIRNELEKTEN---KLEEAQLLVEGMEE-ERIQLERQ------------FRKFK-- 160
Cdd:pfam17380 343 ---------------AMERERELERIRQEERKRELeriRQEEIAMEISRMRElERLQMERQqknervrqeleaARKVKil 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32565466   161 -EEAQQDIDSSSEMVEVLALETEELR----RKVDGPRSESIS----DREDMHEEIEILKAKVAELMKEKEEM 223
Cdd:pfam17380 408 eEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEEERAREMErvrlEEQERQQQVERLRQQEEERKRKKLEL 479
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 17-183 1.95e-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: 40.44  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     17 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERM-------HNLEEQLTDNEDR----FKQLLSDEKARGTESMSRL 85
Cdd:TIGR02169  731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleedlHKLEEALNDLEARlshsRIPEIQAELSKLEEEVSRI 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     86 K---REKELETESWNLKYQMLEK---DLISVKKDAE-RSNEETKRIRN---ELEKTENKLEEAQLLVEGMEEERIQLERQ 155
Cdd:TIGR02169  811 EarlREIEQKLNRLTLEKEYLEKeiqELQEQRIDLKeQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKE 890

                          170       180       190
                   ....*....|....*....|....*....|....
gi 32565466    156 FRKFK------EEAQQDIDSSSEMVEVLALETEE 183
Cdd:TIGR02169  891 RDELEaqlrelERKIEELEAQIEKKRKRLSELKA 924
PLN02939 PLN02939
transferase, transferring glycosyl groups
 20-198 2.17e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 40.27  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   20 SFTKRYSELEERNMSLSDERTRLKTENSVLK---ERMHNLEEQLTDNEDRFKQLlsdeKARGTESMSRLKREKELETESW 96
Cdd:PLN02939 223 SLSKELDVLKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLREL----ESKFIVAQEDVSKLSPLQYDCW 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   97 NLKYQMLEKDLISVKKDAERSN---EETKRIRNELEKTENKLEEAQL------LVEGMEEERIQLERQFRKFKEEAQQDI 167
Cdd:PLN02939 299 WEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVskfssyKVELLQQKLKLLEERLQASDHEIHSYI 378

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 32565466  168 ----DSSSEMVEVLALETEELRRKvdgPRSESISD 198
Cdd:PLN02939 379 qlyqESIKEFQDTLSKLKEESKKR---SLEHPADD 410
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 98-234 2.19e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 2.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  98 LKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKE-----EAQQDIDSSSE 172
Cdd:COG1579  10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyEEQLGNVRNNK 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32565466 173 MVEVLALETEELRRKvdgprsesISDRED----MHEEIEILKAKVAELMKEKEEMTDQLLATSVER 234
Cdd:COG1579  90 EYEALQKEIESLKRR--------ISDLEDeileLMERIEELEEELAELEAELAELEAELEEKKAEL 147
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-241 2.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK--------QLLSDEKARGT 79
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVET 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   80 ESMSRLKREkELETESWNLKYQMLE--------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQ 151
Cdd:PRK02224 470 IEEDRERVE-ELEAELEDLEEEVEEveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  152 LE---RQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPR--SESISDREDMHEEIEILKAKVAELmKEKEEMTDQ 226
Cdd:PRK02224 549 LEaeaEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREAL-AELNDERRE 627

                        250
                 ....*....|....*
gi 32565466  227 LLATSVERGRSLIAD 241
Cdd:PRK02224 628 RLAEKRERKRELEAE 642
PTZ00121 PTZ00121
MAEBL; Provisional
 8-222 3.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMsrlKR 87
Cdd:PTZ00121 1203 EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---RK 1279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    88 EKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKtenKLEEAQLLVEGME---EERIQLERQFRKFKEEAQ 164
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK---KAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   165 QDIDSSSEMVEVLALETEELRRKVDG--PRSESISDREDMHEEIEILKAKVAELMKEKEE 222
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
26-126 3.31e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  26 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDE--KARGTESMSRLKREkeleteswnlkYQML 103
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErrEIRKDREISRLDRE-----------IERL 477

                        90       100
                ....*....|....*....|...
gi 32565466 104 EKDLISVKKDAERSNEETKRIRN 126
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKE 500
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
26-211 3.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   26 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLK------ 99
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRdrleec 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  100 ---YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEM 173
Cdd:PRK02224 334 rvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 32565466  174 VEVLALETEELRRKVDGPRSESISDREDMHEEIEILKA 211
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEA 451
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
115-216 4.33e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 115 ERSNEETKRIRNELEKTENKLEEAqllvegmeEERIQ-LERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKVdgprs 193
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEK--------DERIErLERELSEARSEERREIRKDRE-ISRLDREIERLEREL----- 481

                        90       100
                ....*....|....*....|...
gi 32565466 194 esisdrEDMHEEIEILKAKVAEL 216
Cdd:COG2433 482 ------EEERERIEELKRKLERL 498
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 27-184 4.56e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.11  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    27 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 106
Cdd:pfam07888  70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32565466   107 LisvkkDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEEL 184
Cdd:pfam07888 150 T-----ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 26-222 5.93e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 38.95  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    26 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQL--LSDEKARGTESMSRLKREKELETESWNLKYQML 103
Cdd:pfam05557  30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVISCL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   104 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQ-------------QDI--- 167
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiqsqeQDSeiv 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 32565466   168 -DSSSEMVEVLALETEELRRKVDGPR-SESISDREDMHEEIEILKAKVAELMKEKEE 222
Cdd:pfam05557 190 kNSKSELARIPELEKELERLREHNKHlNENIENKLLLKEEVEDLKRKLEREEKYREE 246
mukB PRK04863
chromosome partition protein MukB;
109-218 6.47e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   109 SVKKDAERSNEETKRIRNELEKTENKLEEAqllvEGMEEERIQLERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKV 188
Cdd:PRK04863  496 DVARELLRRLREQRHLAEQLQQLRMRLSEL----EQRLRQQQRAERLLAEFCKRLGKNLDDEDE-LEQLQEELEARLESL 570

                          90       100       110
                  ....*....|....*....|....*....|
gi 32565466   189 DGPRSESISDREDMHEEIEILKAKVAELMK 218
Cdd:PRK04863  571 SESVSEARERRMALRQQLEQLQARIQRLAA 600
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
105-264 6.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 6.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 105 KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfkEEAQQDIDSSSEMVEVLALETEEL 184
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERL 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466 185 RRKVdgprsESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQ 264
Cdd:COG4717 149 EELE-----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA--ELEEELEEAQEE 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-173 6.87e-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: 38.88  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466      8 EEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKR 87
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     88 EKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeeriQLERQFRKFKEEAQQDI 167
Cdd:TIGR02168  437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALL 512


                   ....*.
gi 32565466    168 DSSSEM 173
Cdd:TIGR02168  513 KNQSGL 518
PRK12704 PRK12704
phosphodiesterase; Provisional
 57-222 7.67e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   57 EEQLTDNEDRFKQLLSDEKAR-----------GTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIR 125
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEaeaikkealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  126 NELEKTENKLEEAQLLVEGMEEEriqLERqfrkfKEEAQQDidsssEMVEVLALETEELRRKVdgprsesisdREDMHEE 205
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEE---LEE-----LIEEQLQ-----ELERISGLTAEEAKEIL----------LEKVEEE 166

                        170
                 ....*....|....*..
gi 32565466  206 ieiLKAKVAELMKEKEE 222
Cdd:PRK12704 167 ---ARHEAAVLIKEIEE 180
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-216 8.08e-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: 38.51  E-value: 8.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466     83 SRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE 162
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 32565466    163 AQQdidsSSEMVEVLALETEELRRKVDgprsESISDREDMHEEIEILKAKVAEL 216
Cdd:TIGR02169  739 LEE----LEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEALNDL 784
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 99-227 8.10e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 8.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466  99 KYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQDID---------- 168
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----AEAEAEIEerreelgera 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565466 169 -------SSSEMVEVL--------ALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 227
Cdd:COG3883  93 ralyrsgGSVSYLDVLlgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
PRK13169 PRK13169
DNA replication initiation control protein YabA;
16-88 8.30e-03

DNA replication initiation control protein YabA;


Pssm-ID: 183876  Cd Length: 110  Bit Score: 35.99  E-value: 8.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32565466   16 NQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDrfkqllSDEKARGTESMSRLKRE 88
Cdd:PRK13169  15 QNLGVLLKELGALKKQLAELLEENTALRLENDKLRERLEELEAEEPAKEK------KKKEGEGKDNLARLYQE 81
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5-165 9.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466    5 FVSEEESKYAMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 84
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565466   85 LKREK-ELETESWNLKYQM--LEKDLISVKKDAE---RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQL-ERQFR 157
Cdd:PRK03918 664 LREEYlELSRELAGLRAELeeLEKRREEIKKTLEklkEELEEREKAKKELEKLEKALERVEELREKVKKYKALLkERALS 743


                 ....*...
gi 32565466  158 KFKEEAQQ 165
Cdd:PRK03918 744 KVGEIASE 751
 
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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