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Conserved domains on  [gi|767939978|ref|XP_011512889|]
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kinesin-like protein KIFC1 isoform X2 [Homo sapiens]

Protein Classification

myosin/kinesin family protein( domain architecture ID 366212)

myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins that provides the driving force in myosin and kinesin mediated processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 250-405 3.00e-90

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


The actual alignment was detected with superfamily member cd01366:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 329  Bit Score: 276.01  E-value: 3.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 250 EKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGAPLSLVDLAGSERLDPGLALGpgerERLRET 329
Cdd:cd01366  178 PEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSERLNKSGATG----DRLKET 253

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939978 330 QAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVI 405
Cdd:cd01366  254 QAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 138-276 1.66e-08

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQaeqgqqeLKNLRACVLELE 217
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLE 881

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVdallHLARQNraVARTAQNERSS 276
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK----RLSELK--AKLEALEEELS 934
 
Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 250-405 3.00e-90

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 276.01  E-value: 3.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 250 EKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGAPLSLVDLAGSERLDPGLALGpgerERLRET 329
Cdd:cd01366  178 PEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSERLNKSGATG----DRLKET 253

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939978 330 QAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVI 405
Cdd:cd01366  254 QAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
Kinesin pfam00225
Kinesin motor domain;
252-403 4.60e-64

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 208.20  E-value: 4.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  252 EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEH---SSRGLQCGAPLSLVDLAGSERLDpglALGPGERERLRE 328
Cdd:pfam00225 174 EVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNrstGGEESVKTGKLNLVDLAGSERAS---KTGAAGGQRLKE 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939978  329 TQAINSSLSTLGLVIMALSNKES-HVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQC 403
Cdd:pfam00225 251 AANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 252-406 7.11e-61

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 200.49  E-value: 7.11e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   252 EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGE--HSSRGLQCGAPLSLVDLAGSERLDPGLALGpgerERLRET 329
Cdd:smart00129 177 EVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSERAKKTGAEG----DRLKEA 252

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978   330 QAINSSLSTLGLVIMALSN--KESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIG 406
Cdd:smart00129 253 GNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
226-399 2.22e-36

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 139.87  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 226 LVQELQKKQVELQEERRGLMSQLEEK------EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGA 299
Cdd:COG5059  155 LSPNEESLNIREDSLLGVKVAGLTEKhvsskeEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETS 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 300 PLSLVDLAGSERLDPGLALGpgerERLRETQAINSSLSTLGLVIMALSNK--ESHVPYRNSKLTYLLQNSLGGSAKMLMF 377
Cdd:COG5059  235 KLSLVDLAGSERAARTGNRG----TRLKEGASINKSLLTLGNVINALGDKkkSGHIPYRESKLTRLLQDSLGGNCNTRVI 310

                        170       180
                 ....*....|....*....|..
gi 767939978 378 VNISPLEENVSESLNSLRFASK 399
Cdd:COG5059  311 CTISPSSNSFEETINTLKFASR 332
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 251-399 1.71e-23

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 103.48  E-value: 1.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  251 KEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISG--EHSSRGLQC--GAPLSLVDLAGSERLDPGLALGpgerERL 326
Cdd:PLN03188  277 KDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESrcKSVADGLSSfkTSRINLVDLAGSERQKLTGAAG----DRL 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767939978  327 RETQAINSSLSTLGLVIMAL-----SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 399
Cdd:PLN03188  353 KEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQR 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-276 1.66e-08

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: 56.61  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQaeqgqqeLKNLRACVLELE 217
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLE 881

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVdallHLARQNraVARTAQNERSS 276
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK----RLSELK--AKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-286 1.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 145 DLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQE 224
Cdd:COG1196  250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939978 225 GLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQI 286
Cdd:COG1196  330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 142-231 7.30e-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: 41.16  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  142 QLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKnlracvlELEERLS 221
Cdd:pfam04849 218 QMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQ-------ELQDRYA 290

                          90
                  ....*....|
gi 767939978  222 TQEGLVQELQ 231
Cdd:pfam04849 291 ECLGMLHEAQ 300
 
Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 250-405 3.00e-90

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 276.01  E-value: 3.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 250 EKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGAPLSLVDLAGSERLDPGLALGpgerERLRET 329
Cdd:cd01366  178 PEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSERLNKSGATG----DRLKET 253

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939978 330 QAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVI 405
Cdd:cd01366  254 QAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
Kinesin pfam00225
Kinesin motor domain;
252-403 4.60e-64

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 208.20  E-value: 4.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  252 EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEH---SSRGLQCGAPLSLVDLAGSERLDpglALGPGERERLRE 328
Cdd:pfam00225 174 EVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNrstGGEESVKTGKLNLVDLAGSERAS---KTGAAGGQRLKE 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767939978  329 TQAINSSLSTLGLVIMALSNKES-HVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQC 403
Cdd:pfam00225 251 AANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 252-406 7.11e-61

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 200.49  E-value: 7.11e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   252 EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGE--HSSRGLQCGAPLSLVDLAGSERLDPGLALGpgerERLRET 329
Cdd:smart00129 177 EVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSERAKKTGAEG----DRLKEA 252

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978   330 QAINSSLSTLGLVIMALSN--KESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIG 406
Cdd:smart00129 253 GNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 226-400 3.82e-56

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 187.85  E-value: 3.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 226 LVQELQKKQVELQE--ERRGLMSQLEEKEVD------ALLHLARQNRAVARTAQNERSSRSHSVFQLQIsgeHSSRGLQC 297
Cdd:cd00106  144 LLSPVPKKPLSLREdpKRGVYVKGLTEVEVGsledalELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV---KQRNREKS 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 298 GAP-----LSLVDLAGSERLDPGLAlgpgERERLRETQAINSSLSTLGLVIMALS-NKESHVPYRNSKLTYLLQNSLGGS 371
Cdd:cd00106  221 GESvtsskLNLVDLAGSERAKKTGA----EGDRLKEGGNINKSLSALGKVISALAdGQNKHIPYRDSKLTRLLQDSLGGN 296

                        170       180
                 ....*....|....*....|....*....
gi 767939978 372 AKMLMFVNISPLEENVSESLNSLRFASKV 400
Cdd:cd00106  297 SKTIMIACISPSSENFEETLSTLRFASRA 325
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 226-402 9.30e-46

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 160.70  E-value: 9.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 226 LVQELQKKQVELQEER-RGL----MSQL---EEKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQIS----GEHSSR 293
Cdd:cd01371  149 LLGKDQTKRLELKERPdTGVyvkdLSMFvvkNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEcsekGEDGEN 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 294 GLQCGApLSLVDLAGSERLDPGLALGpgerERLRETQAINSSLSTLGLVIMAL-SNKESHVPYRNSKLTYLLQNSLGGSA 372
Cdd:cd01371  229 HIRVGK-LNLVDLAGSERQSKTGATG----ERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNS 303

                        170       180       190
                 ....*....|....*....|....*....|
gi 767939978 373 KMLMFVNISPLEENVSESLNSLRFASKVNQ 402
Cdd:cd01371  304 KTVMCANIGPADYNYDETLSTLRYANRAKN 333
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 227-399 1.16e-40

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 146.71  E-value: 1.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 227 VQELQKKQVELQEERRGLMSQLEEkevdallhlarqNRAVARTAQNERSSRSHSVFQLQIsgEHSSRGLQCGAP-----L 301
Cdd:cd01374  156 VAGLTEEIVSSPEHALSLIARGEK------------NRHVGETDMNERSSRSHTIFRITI--ESSERGELEEGTvrvstL 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 302 SLVDLAGSERLDPGLALGpgerERLRETQAINSSLSTLGLVIMALSNKES--HVPYRNSKLTYLLQNSLGGSAKMLMFVN 379
Cdd:cd01374  222 NLIDLAGSERAAQTGAAG----VRRKEGSHINKSLLTLGTVISKLSEGKVggHIPYRDSKLTRILQPSLGGNSRTAIICT 297

                        170       180
                 ....*....|....*....|
gi 767939978 380 ISPLEENVSESLNSLRFASK 399
Cdd:cd01374  298 ITPAESHVEETLNTLKFASR 317
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 250-402 2.10e-40

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 146.32  E-value: 2.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 250 EKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGAPLSLVDLAGSERLDPGLALGpgerERLRET 329
Cdd:cd01369  175 PEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKTGAEG----AVLDEA 250

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767939978 330 QAINSSLSTLGLVIMALSNKE-SHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQ 402
Cdd:cd01369  251 KKINKSLSALGNVINALTDGKkTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKT 324
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 251-411 1.49e-39

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 144.80  E-value: 1.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 251 KEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQ-----------ISGEHSSRglqcgapLSLVDLAGSERLDPGLALG 319
Cdd:cd01365  194 EDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVltqkrhdaetnLTTEKVSK-------ISLVDLAGSERASSTGATG 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 320 pgerERLRETQAINSSLSTLGLVIMAL--------SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESL 391
Cdd:cd01365  267 ----DRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETL 342

                        170       180
                 ....*....|....*....|
gi 767939978 392 NSLRFASKVNQCViGTAQAN 411
Cdd:cd01365  343 STLRYADRAKKIV-NRAVVN 361
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 232-397 1.53e-38

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 141.70  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 232 KKQVELQEERRG--LMSQLEEKEV----DALLHLAR--QNRAVARTAQNERSSRSHSVFQLQISGEH----------SSR 293
Cdd:cd01372  152 KPTISIREDSKGgiTIVGLTEVTVlsaeDMMSCLEQgsLSRTTASTAMNSQSSRSHAIFTITLEQTKkngpiapmsaDDK 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 294 GLQCGAPLSLVDLAGSERLDPGLALGpgerERLRETQAINSSLSTLGLVIMAL---SNKESHVPYRNSKLTYLLQNSLGG 370
Cdd:cd01372  232 NSTFTSKFHFVDLAGSERLKRTGATG----DRLKEGISINSGLLALGNVISALgdeSKKGAHVPYRDSKLTRLLQDSLGG 307

                        170       180
                 ....*....|....*....|....*..
gi 767939978 371 SAKMLMFVNISPLEENVSESLNSLRFA 397
Cdd:cd01372  308 NSHTLMIACVSPADSNFEETLNTLKYA 334
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 215-399 1.10e-36

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 137.07  E-value: 1.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 215 ELEERLSTQEGLVQELQkkQVELQEERRGLMSQ-LEE------KEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQIS 287
Cdd:cd01364  152 ELFDLLSPSSDVSERLR--MFDDPRNKRGVIIKgLEEitvhnkDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIH 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 288 -GEHSSRG---LQCGApLSLVDLAGSERLDPGLAlgpgERERLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYL 363
Cdd:cd01364  230 iKETTIDGeelVKIGK-LNLVDLAGSENIGRSGA----VDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRL 304

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767939978 364 LQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 399
Cdd:cd01364  305 LQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHR 340
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
226-399 2.22e-36

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 139.87  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 226 LVQELQKKQVELQEERRGLMSQLEEK------EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGA 299
Cdd:COG5059  155 LSPNEESLNIREDSLLGVKVAGLTEKhvsskeEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETS 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 300 PLSLVDLAGSERLDPGLALGpgerERLRETQAINSSLSTLGLVIMALSNK--ESHVPYRNSKLTYLLQNSLGGSAKMLMF 377
Cdd:COG5059  235 KLSLVDLAGSERAARTGNRG----TRLKEGASINKSLLTLGNVINALGDKkkSGHIPYRESKLTRLLQDSLGGNCNTRVI 310

                        170       180
                 ....*....|....*....|..
gi 767939978 378 VNISPLEENVSESLNSLRFASK 399
Cdd:COG5059  311 CTISPSSNSFEETINTLKFASR 332
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 252-400 1.08e-32

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 126.08  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 252 EVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCG--APLSLVDLAGSERLDPGLAlgpgERERLRET 329
Cdd:cd01373  184 DVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVNIrtSRLNLVDLAGSERQKDTHA----EGVRLKEA 259

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939978 330 QAINSSLSTLGLVIMALSN----KESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKV 400
Cdd:cd01373  260 GNINKSLSCLGHVINALVDvahgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRA 334
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 242-400 4.10e-32

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 124.23  E-value: 4.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 242 RGLMSQLEEKEVDA--LLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQ--CGAPLSLVDLAGSERLDPGLA 317
Cdd:cd01375  174 KGLSLHLTSQEEEAlsLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEkyITSKLNLVDLAGSERLSKTGV 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 318 LGpgerERLRETQAINSSLSTLGLVIMALSNKE-SHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRF 396
Cdd:cd01375  254 EG----QVLKEATYINKSLSFLEQAIIALSDKDrTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRF 329


                 ....
gi 767939978 397 ASKV 400
Cdd:cd01375  330 ASRV 333
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 251-401 2.63e-31

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 122.07  E-value: 2.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 251 KEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCG---APLSLVDLAGSERLDPGLALGpgerERLR 327
Cdd:cd01370  191 EEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQvrqGKLSLIDLAGSERASATNNRG----QRLK 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939978 328 ETQAINSSLSTLGLVIMALSN---KESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVN 401
Cdd:cd01370  267 EGANINRSLLALGNCINALADpgkKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAK 343
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 251-397 6.12e-31

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 121.35  E-value: 6.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 251 KEVDALLHLARQNRAVARTAQNERSSRSHSVFQ---LQISGEHSSRGLQCG-----APLSLVDLAGSERLDPGLALGpge 322
Cdd:cd01368  186 EEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTiklVQAPGDSDGDVDQDKdqitvSQLSLVDLAGSERTSRTQNTG--- 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 323 rERLRETQAINSSLSTLGLVIMALSNKE-----SHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFA 397
Cdd:cd01368  263 -ERLKEAGNINTSLMTLGTCIEVLRENQlqgtnKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 229-401 1.06e-30

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 119.91  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 229 ELQKKQVELQEERRG--LMSQLEEKEVDALLHL------ARQNRAVARTAQNERSSRSHSVFQLQ-ISGEHSSRGLQCGA 299
Cdd:cd01376  142 EPASKELVIREDKDGniLIPGLSSKPIKSMAEFeeaflpASKNRTVAATRLNDNSSRSHAVLLIKvDQRERLAPFRQRTG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 300 PLSLVDLAGSE---RLDpglalgpGERERLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLM 376
Cdd:cd01376  222 KLNLIDLAGSEdnrRTG-------NEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIM 294

                        170       180
                 ....*....|....*....|....*
gi 767939978 377 FVNISPLEENVSESLNSLRFASKVN 401
Cdd:cd01376  295 VANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 264-400 1.13e-28

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 114.70  E-value: 1.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 264 RAVARTAQNERSSRSHSVFQLQISgehSSRGLQCGAPLSLVDLAGSERldpGLALGPGERERLRETQAINSSLSTLGLVI 343
Cdd:cd01367  196 RTTGQTSANSQSSRSHAILQIILR---DRGTNKLHGKLSFVDLAGSER---GADTSSADRQTRMEGAEINKSLLALKECI 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939978 344 MALSNKESHVPYRNSKLTYLLQNSL-GGSAKMLMFVNISPLEENVSESLNSLRFASKV 400
Cdd:cd01367  270 RALGQNKAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRV 327
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 251-399 1.71e-23

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 103.48  E-value: 1.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  251 KEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISG--EHSSRGLQC--GAPLSLVDLAGSERLDPGLALGpgerERL 326
Cdd:PLN03188  277 KDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESrcKSVADGLSSfkTSRINLVDLAGSERQKLTGAAG----DRL 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767939978  327 RETQAINSSLSTLGLVIMAL-----SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 399
Cdd:PLN03188  353 KEAGNINRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQR 430
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
140-346 5.39e-09

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 57.83  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 140 KGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEghlakvQAQAEQGQQELKNLRACVLELEER 219
Cdd:COG5059  372 REQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIISGTFERKKLL------KEEGWKYKSTLQFLRIEIDRLLLL 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 220 LSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQ-NRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCg 298
Cdd:COG5059  446 REEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKASkLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELS- 524

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767939978 299 apLSLVDLAGSERLdPGLALGpgerERLRETQAINSSLSTLGLVIMAL 346
Cdd:COG5059  525 --LNQVDLAGSERK-VSQSVG----ELLRETQSLNKSLSSLGDVIHAL 565
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-276 1.66e-08

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: 56.61  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQaeqgqqeLKNLRACVLELE 217
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLE 881

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVdallHLARQNraVARTAQNERSS 276
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK----RLSELK--AKLEALEEELS 934
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 250-345 7.77e-08

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 51.58  E-value: 7.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 250 EKEVDALLHLARQNRaVARTAQNERSSRSHSVFQLqisgehssrglqcgaplsLVDLAGSERldpglalgpgererlret 329
Cdd:cd01363  103 EDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFEI------------------ 145

                         90
                 ....*....|....*.
gi 767939978 330 qaINSSLSTLGLVIMA 345
Cdd:cd01363  146 --INESLNTLMNVLRA 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-278 3.12e-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: 52.75  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVdallHLARQNRAVARTAQNERSSRS 278
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLK 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-286 1.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 145 DLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQE 224
Cdd:COG1196  250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939978 225 GLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQI 286
Cdd:COG1196  330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 145-328 2.90e-06

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: 49.67  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   145 DLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQE 224
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   225 GLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTaqnERSSRSHSVFQLQISGEHSSRGLQCGAPLSlv 304
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLKKLEEAELKELQ-- 439

                          170       180
                   ....*....|....*....|....
gi 767939978   305 dlAGSERLDPGLALGPGERERLRE 328
Cdd:TIGR02168  440 --AELEELEEELEELQEELERLEE 461
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-274 5.48e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 145 DLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQE 224
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767939978 225 GLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNER 274
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-277 7.85e-06

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: 48.13  E-value: 7.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   142 QLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLS 221
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939978   222 TQEGLVQELQKKQVELQEERRGLMSQLEEK-----EVDALLHLARQNRAVARTAQNERSSR 277
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALlneraSLEEALALLRSELEELSEELRELESK 909
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-274 1.99e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:COG4372   63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939978 218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLH-LARQNRAVARTAQNER 274
Cdd:COG4372  143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaLDELLKEANRNAEKEE 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-274 2.16e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 146 LNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEG 225
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767939978 226 LVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNER 274
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-274 2.39e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 145 DLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQE 224
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767939978 225 GLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNER 274
Cdd:COG1196  365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-276 4.07e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   147 NAELKRCRERTQtldqenqQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGL 226
Cdd:TIGR02168  676 RREIEELEEKIE-------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767939978   227 VQELQKKQVELQEERRGLMSQLEEKEVDALLHLAR--QNRAVARTAQNERSS 276
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKA 800
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
130-277 4.30e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 130 KPSKRPAWDLKGQLCDLNAELKRCRERT---QTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQ--Q 204
Cdd:COG4717   60 KPQGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleA 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939978 205 ELKNLRACVLELEERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNERSSR 277
Cdd:COG4717  140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-275 4.63e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 4.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEvDALLHLARQNRAVARTAQNERS 275
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELE-AELEELESRLEELEEQLETLRS 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
148-331 5.99e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  148 AELKRCRERTQTLDQENQQLQdQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELknLRACVLELEERLSTQEGLV 227
Cdd:COG4913   235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAEL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  228 QELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAvARTAQNERSSRSHSVfqlqisgEHSSRGLQCGAPLSLVDL- 306
Cdd:COG4913   312 ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIER-LERELEERERRRARL-------EALLAALGLPLPASAEEFa 383

                         170       180
                  ....*....|....*....|....*
gi 767939978  307 AGSERLDPGLALGPGERERLRETQA 331
Cdd:COG4913   384 ALRAEAAALLEALEEELEALEEALA 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 148-273 8.47e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 148 AELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGLV 227
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767939978 228 QELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNE 273
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-275 1.03e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQlRDAQQQVKALGTERTTLEGHLAKVQAQAEQgqqeLKNLRAC---VL 214
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAE----LERLDASsddLA 688

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939978  215 ELEERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNERS 275
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-252 1.89e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:COG4372   49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767939978 218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKE 252
Cdd:COG4372  129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-252 3.59e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQ-QQVKALGTERTTLEGHLAKVQAQAEQGQQELKNL------- 209
Cdd:COG4913   299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALglplpas 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767939978  210 ----RACVLELEERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKE 252
Cdd:COG4913   379 aeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
139-276 4.45e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  139 LKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTER-TTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALG 372

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978  218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAvARTAQNERSS 276
Cdd:COG4913   373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-LRELEAEIAS 430
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 142-231 7.30e-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: 41.16  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  142 QLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKnlracvlELEERLS 221
Cdd:pfam04849 218 QMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQ-------ELQDRYA 290

                          90
                  ....*....|
gi 767939978  222 TQEGLVQELQ 231
Cdd:pfam04849 291 ECLGMLHEAQ 300
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
136-262 9.17e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 9.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 136 AWDLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEghlAKVQAQAEQGQQELKNLRACVLE 215
Cdd:COG4717  127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEE 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767939978 216 LEERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQ 262
Cdd:COG4717  204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-296 9.85e-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: 9.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEEkevdallhLARQnravARTAQNERSSRSHSVFQLQISGEHSSRGLQ 296
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLED--------LEEQ----IEELSEDIESLAAEIEELEELIEELESELE 876
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 168-274 1.14e-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: 40.90  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 168 QDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGLVQELQKKQVELQEERRGLMSQ 247
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100
                 ....*....|....*....|....*..
gi 767939978 248 LEEKEVDallhLARQNRAVARTAQNER 274
Cdd:COG4942   99 LEAQKEE----LAELLRALYRLGRQPP 121
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-262 1.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  138 DLKGQLCDLNAELKRCRERTQTLDQEN-QQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLEL 216
Cdd:COG4913   313 RLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  217 EERLSTQEGLVQE-----------LQKKQVELQEERRGL---MSQLEEKEVDALLHLARQ 262
Cdd:COG4913   393 LEALEEELEALEEalaeaeaalrdLRRELRELEAEIASLerrKSNIPARLLALRDALAEA 452
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-277 1.46e-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: 40.82  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNaelKRCRERTQTLDQENQQLQDQLRDAQQQVKalgTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:TIGR02169  255 KLTEEISELE---KRLEEIEQLLEELNKKIKDLGEEEQLRVK---EKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939978   218 ERLSTQEGLVQELQKKQVELQEERRGLMSQLEE--KEVDALLHLARQNRAVARTAQNERSSR 277
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAElkEELEDLRAELEEVDKEFAETRDELKDY 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-274 2.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 165 QQLQDQLRDAQQQVKALgtERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGLVQELQKKQVELQEERRGL 244
Cdd:COG1196  216 RELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100       110
                 ....*....|....*....|....*....|
gi 767939978 245 MSQLEEKEVDALLHLARQNRAVARTAQNER 274
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEE 323
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
145-252 2.24e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 145 DLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQE 224
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90       100
                 ....*....|....*....|....*...
gi 767939978 225 GLVQELQKKQVELQEERRGLMSQLEEKE 252
Cdd:COG4372  122 KERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-273 3.18e-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: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   142 QLCDLNAELKRCRERTQT---LDQENQQLQDQLRDAQQQVkaLGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEE 218
Cdd:TIGR02168  190 RLEDILNELERQLKSLERqaeKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEE 267

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767939978   219 RLSTQEGLVQELQKKQVELQEERRGLMSQLEEKEVDALLHLARQNRAVARTAQNE 273
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 139-251 4.23e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978  139 LKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTErttLEGHlakvqaqaEQGQQELKNLRACVLELEE 218
Cdd:pfam13851  31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQ---LENY--------EKDKQSLKNLKARLKVLEK 99

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767939978  219 RLSTQEGLVQELQKKQVELQEERRGLMSQLEEK 251
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFEKVERERDELYDKFEAA 132
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 155-248 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: 38.59  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 155 ERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGLVQELQKKQ 234
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90
                 ....*....|....
gi 767939978 235 VELQEERRGLMSQL 248
Cdd:COG4942  100 EAQKEELAELLRAL 113
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 146-269 9.04e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978 146 LNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRAC------------- 212
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeiesl 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767939978 213 ----------VLELEERLSTQEGLVQELQKKQVELQEERRGLMSQLEE--KEVDALLHLARQNRAVART 269
Cdd:COG1579  102 krrisdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEelAELEAELEELEAEREELAA 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-250 9.51e-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: 38.50  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939978   138 DLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELE 217
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767939978   218 ERLstqeglvQELQKKQVELQEERRGLMSQLEE 250
Cdd:TIGR02168  915 REL-------EELREKLAQLELRLEGLEVRIDN 940
 
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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