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Conserved domains on  [gi|1370514033|ref|XP_024303221|]
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zinc-regulated GTPase metalloprotein activator 1E isoform X7 [Homo sapiens]

Protein Classification

CobW family GTP-binding protein( domain architecture ID 11424901)

CobW family GTP-binding protein similar to GTPase CobW, which is involved in the synthesis of cobalamin, and zinc-binding GTPase YeiR which belongs to the G3E family of P-loop GTPases

Gene Ontology:  GO:0005525|GO:0003924|GO:0046872
PubMed:  34302342|11916378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
 3-250 2.39e-55

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


:

Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 180.75  E-value: 2.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   3 KKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVALADIILINKT 82
Cdd:COG0523    82 RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAFADVIVLNKT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033  83 DLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQhvPGTQPHLDQSIVTITFEVPGNA 162
Cdd:COG0523   159 DLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE--ELRDHEHDDGIRSFVFRSDRPF 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033 163 KEEHLNMFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPvSWKDDtERTNRLVLIGRNLD 242
Cdd:COG0523   237 DPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLVFIGRDLD 302


                  ....*...
gi 1370514033 243 KDILKQLF 250
Cdd:COG0523   303 EAALEAAL 310
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
 3-250 2.39e-55

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 180.75  E-value: 2.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   3 KKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVALADIILINKT 82
Cdd:COG0523    82 RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAFADVIVLNKT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033  83 DLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQhvPGTQPHLDQSIVTITFEVPGNA 162
Cdd:COG0523   159 DLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE--ELRDHEHDDGIRSFVFRSDRPF 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033 163 KEEHLNMFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPvSWKDDtERTNRLVLIGRNLD 242
Cdd:COG0523   237 DPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLVFIGRDLD 302


                  ....*...
gi 1370514033 243 KDILKQLF 250
Cdd:COG0523   303 EAALEAAL 310
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 1-123 1.22e-47

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 157.30  E-value: 1.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   1 MQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADIILIN 80
Cdd:cd03112    79 LERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVLN 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370514033  81 KTDLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLH 123
Cdd:cd03112   156 KTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 1-108 6.76e-23

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 92.32  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   1 MQKKGKFDDILLETTGLADPGAVTSMFWVDaELGSDIYLDGIITIVDSKyglkHLTEEKPdgLINEATRQVALADIILIN 80
Cdd:pfam02492  78 LEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDAA----NEADGEK--IPRKAGDQIAFADLIVLN 150

                          90       100
                  ....*....|....*....|....*....
gi 1370514033  81 KTDLVPEE-DVKKLRTTIRSINGLGQILE 108
Cdd:pfam02492 151 KTDLAPEVaLLEVLEEDLRRLNPGAPVVP 179
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
 7-252 1.38e-18

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 83.60  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   7 FDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpdglINEATRQVALADIILINKTDLVP 86
Cdd:PRK11537   91 FDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQVGYADRILLTKTDVAG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033  87 EEDvkKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAF---DSLsgISLQKKLQHVPGTQPHLdQSIVtITFEVPGNAK 163
Cdd:PRK11537  165 EAE--KLRERLARINARAPVYTVVHGDIDLSLLFNTNGFmleENV--VSTKPRFHFIADKQNDI-SSIV-VELDYPVDIS 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033 164 EehLNMFIQNLLweknVRNKDNhcmeVIRLKGLVSIKDKSQQVIVQGVHELYDLEetpvsWK---DDTERTNRLVLIGRN 240
Cdd:PRK11537  239 E--VSRVMENLL----LESADK----LLRYKGMLWIDGEPNRLLFQGVQRLYSAD-----WDrpwGDETPHSTLVFIGIQ 303

                         250
                  ....*....|..
gi 1370514033 241 LDKDILKQLFIA 252
Cdd:PRK11537  304 LPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
 190-250 4.90e-08

Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.


Pssm-ID: 214844 [Multi-domain]  Cd Length: 92  Bit Score: 49.52  E-value: 4.90e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370514033  190 VIRLKGLVSIKDKSQQVIV-QGVHELYDLEETPVsWKDDTERTNRLVLIGRNLDKDILKQLF 250
Cdd:smart00833  28 VLRAKGFFWLASRPDLPGVlSQAGGRLRIEPAGA-WPAAGDRRTRLVFIGRDLDEEAIRAAL 88
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
 3-250 2.39e-55

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 180.75  E-value: 2.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   3 KKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVALADIILINKT 82
Cdd:COG0523    82 RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAFADVIVLNKT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033  83 DLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQhvPGTQPHLDQSIVTITFEVPGNA 162
Cdd:COG0523   159 DLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE--ELRDHEHDDGIRSFVFRSDRPF 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033 163 KEEHLNMFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPvSWKDDtERTNRLVLIGRNLD 242
Cdd:COG0523   237 DPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLVFIGRDLD 302


                  ....*...
gi 1370514033 243 KDILKQLF 250
Cdd:COG0523   303 EAALEAAL 310
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 1-123 1.22e-47

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 157.30  E-value: 1.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   1 MQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADIILIN 80
Cdd:cd03112    79 LERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVLN 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370514033  81 KTDLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLH 123
Cdd:cd03112   156 KTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 1-108 6.76e-23

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 92.32  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   1 MQKKGKFDDILLETTGLADPGAVTSMFWVDaELGSDIYLDGIITIVDSKyglkHLTEEKPdgLINEATRQVALADIILIN 80
Cdd:pfam02492  78 LEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDAA----NEADGEK--IPRKAGDQIAFADLIVLN 150

                          90       100
                  ....*....|....*....|....*....
gi 1370514033  81 KTDLVPEE-DVKKLRTTIRSINGLGQILE 108
Cdd:pfam02492 151 KTDLAPEVaLLEVLEEDLRRLNPGAPVVP 179
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
 151-250 1.23e-19

Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of putative metal chaperones that can be separated into up to 15 subgroups. In addition to known roles in cobalamin biosynthesis and the activation of the Fe-type nitrile hydratase, this family is also known to be involved in the response to zinc limitation. The CobW subgroup involved in cobalamin synthesis represents only a small sub-fraction of the family.


Pssm-ID: 462228 [Multi-domain]  Cd Length: 93  Bit Score: 81.13  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033 151 IVTITFEVPGNAKEEHLNMFIQNLLWEKNVrnkdnhcmevIRLKGLVSIKDKSQQVIVQGVHELYDLEETPVSWKDDtER 230
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69

                          90       100
                  ....*....|....*....|
gi 1370514033 231 TNRLVLIGRNLDKDILKQLF 250
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAAL 89
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
 7-252 1.38e-18

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 83.60  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033   7 FDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpdglINEATRQVALADIILINKTDLVP 86
Cdd:PRK11537   91 FDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQVGYADRILLTKTDVAG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033  87 EEDvkKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAF---DSLsgISLQKKLQHVPGTQPHLdQSIVtITFEVPGNAK 163
Cdd:PRK11537  165 EAE--KLRERLARINARAPVYTVVHGDIDLSLLFNTNGFmleENV--VSTKPRFHFIADKQNDI-SSIV-VELDYPVDIS 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370514033 164 EehLNMFIQNLLweknVRNKDNhcmeVIRLKGLVSIKDKSQQVIVQGVHELYDLEetpvsWK---DDTERTNRLVLIGRN 240
Cdd:PRK11537  239 E--VSRVMENLL----LESADK----LLRYKGMLWIDGEPNRLLFQGVQRLYSAD-----WDrpwGDETPHSTLVFIGIQ 303

                         250
                  ....*....|..
gi 1370514033 241 LDKDILKQLFIA 252
Cdd:PRK11537  304 LPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
 190-250 4.90e-08

Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.


Pssm-ID: 214844 [Multi-domain]  Cd Length: 92  Bit Score: 49.52  E-value: 4.90e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370514033  190 VIRLKGLVSIKDKSQQVIV-QGVHELYDLEETPVsWKDDTERTNRLVLIGRNLDKDILKQLF 250
Cdd:smart00833  28 VLRAKGFFWLASRPDLPGVlSQAGGRLRIEPAGA-WPAAGDRRTRLVFIGRDLDEEAIRAAL 88
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
 73-109 1.80e-04

Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion transport and metabolism];


Pssm-ID: 441959  Cd Length: 441  Bit Score: 42.52  E-value: 1.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1370514033  73 LADIILINKTDLVPEEDVKKLRTTIRSINGLGQILET 109
Cdd:COG2403   261 MADVVVINKVDTADPEDIETVRENIRKVNPKAEIIEA 297
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 71-109 1.92e-03

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 38.50  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370514033  71 VALADIILINKTDLVP--EEDVKKLRTTIRSINGLGQILET 109
Cdd:COG0378   138 FTAADLLVINKIDLAPyvGFDLEVMEEDARRVNPGAPIFEV 178
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
 74-109 6.84e-03

nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases.


Pssm-ID: 349775  Cd Length: 203  Bit Score: 36.81  E-value: 6.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370514033  74 ADIILINKTDLVP--EEDVKKLRTTIRSINGLGQILET 109
Cdd:cd05390   149 ADVVLINKIDLLPyfDFDVEKAKEDIKKLNPNAPIIEV 186
 
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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